CYANOBACTERIAL AND PLANT ACETYL-CoA CARBOXYLASE

Abstract: The present invention provides isolated and purified polynucleotides that encode plant and cyanobacterial polypeptides that participate in the carboxylation of acetyl-CoA. Isolated cyanobacterial and plant polypeptides that catalyze acetyl-CoA carboxylation are also provided. Processes for altering acetyl-CoA carboxylation, increasing herbicide resistance of plants and identifying herbicide resistant variants of acetyl-CoA carboxylase are also provided.

Description: CYANOBACTERIALANDPLANT ACETYL-CoA CARBOXYLASE Description Technical Field of the Invention The present invention relates to polynucleotides and polypeptides of acetyl-CoA carboxylase in cyanobacteria and plants. Polynucleotides encoding acetyl-CoA carboxylase have use in conferring herbicide resistance and in determining the herbicide resistance of plants in a breeding program. Background of the Invention Acetyl-CoA carboxylase (ACC) is the first enzyme of the biosynthetic pathway to fatty acids. It belongs to a group of carboxylases that use biotin as cofactor and bicarbonate as a source of the carboxyl group. ACC catalyzes the addition of CO 2 to acetyl-CoA to yield malonyl-CoA in two steps as shown below. BCCP + ATP + HCO. 3 → BCCP-CO 2 + ADP + P* (1) BCCP-CO 2 + Acetyl-CoA → BCCP + malonyl-CoA (2) First, biotin becomes carboxylated at the expense of ATP. The carboxyl group is then transferred to Ac-CoA [Knowles, 1989]. This irreversible reaction is the committed step in fatty acid synthesis and is a target for multiple regulatory mechanisms. Reaction (1) is catalyzed by biotin carboxylase (BC); reaction (2) by transcarboxylase (TC); BCCP = biotin carboxyl carrier protein. ACC purified from E.coli contains three distinct, separable components.: biotin carboxylase (BC), a dimer of 49-kD monomers, biotin carboxyl carrier protein (BCCP) a dimer of 17-kD monomers and transcarboxylase (TC), a tetramer containing two each of 33-kD and 35-kD subunits. The biotin prosthetic group is covalently attached to the 7-amino group of a lysine residue of BCCP. The primary structure of E.coli BCCP and BC is known (fabE and fabG genes,respectively, have been cloned and sequenced) [Alix, 1989; Maramatsu, et al., 1989; Li, et al., 1992]. In bacteria, fatty acids are primarily precursors of phospholipids rather than storage fuels, and so ACC activity is coordinated with cell growth and division. Rat and chicken ACC consist of a dimer of about 265 kD (rat has also a 280 kD isoform) subunits that contains all of the bacterial enzyme activities. Both mammalian and avian ACC are cytoplasmic enzymes and their substrate is transported out of mitochondria via citrate. ACC content and/or activity varies with the rate of fatty acid synthesis or energy requirements in different nutritional, hormonal and developmental states. ACC mRNA is transcribed using different promoters and can be regulated by alternative splicing. ACC catalytic activity is regulated allosterically by a number of metabolites and by reversible phosphorylation of the enzyme. The primary structure of rat and chicken enzymes, and the primary structure of the 5 '-untranslated region of mRNA have been deduced from cDNA sequences [Lopez-Casillas, et al., 1988; Takai, et al., 1988]. The primary structure of yeast ACC has also been determined [Feel, et al., 1992]. Studies on plant ACC are far less advanced [Harwood, 1988]. It was originally thought that plant ACC consisted of low molecular weight dissociable subunits similar to those of bacteria. Those results appeared to be due to degradation of the enzyme during purification. More recent results indicate that the wheat enzyme, as well as those from parsley and rape, are composed of two about 220 kD monomers, similar to the enzyme from rat and chicken [Harwood, 1988; Egin-Buhler, et al., 1983; Wurtelle, et al., 1990; Slabas, et al., 1985]. The plant ACC is located entirely in the stroma of plastids, where all plant fatty acid synthesis occurs. No plant gene encoding ACC has been reported to date. The gene must be nuclear because no corresponding sequence is seen in the complete chloroplast DNA sequences of tobacco, liverwort or rice. ACC, like the vast majority of chloroplast proteins which are encoded in nuclear DNA, must be synthesized in the cytoplasm and then transported into the chloroplast, probably requiring a chloroplast transport sequence. Although the basic features of plant ACC must be the same as those of prokaryotic and other eucaryotic ACCs, significant differences can be also expected due, for example, to differences in plant cell metabolism and ACC cellular localization. Structural similarities deduced from the available amino acid sequences suggest strong evolutionary conservation among biotin carboxylases and biotin carboxylase domains of all biotin-dependent carboxylases. On the contrary, the BCCP domains show very little conservation outside the sequence E(A/V)MKM (lysine residue is biotinylated) which is found in all biotinylated proteins including pyruvate carboxylase and propionyl-CoA carboxylase [Knowles, 1989; Samols, et al., 1988]. It is likely that the three functional domains of ACC located in E.coli on separate polypeptides are present in carboxylases containing two (human propionyl-CoA carboxylase) or only one (yeast pyruvate carboxylase, mammalian, avian and probably also plant ACC) polypeptide as a result of gene fusion during evolution. Several years ago it was shown that aryloxyphenoxypropionates and cyclohexanediones, powerful herbicides effective against monocot weeds, inhibit fatty acid biosynthesis in sensitive plants. Recently it has been determined that ACC is the target enzyme for both of these classes of herbicide. Dicotyledonous plants are resistant to these compounds, as are other eukaryotes and prokaryotes. The mechanisms of inhibition and resistance of the enzyme are not known [Lichtenthaler, 1990]. It has occurred to others that the evolutionary relatedness of cyanobacteria and plants make the former useful sources of cloned genes for the isolation of plant cDNAs. For example, Pecker et al used the cloned gene for the enzyme phytoene desaturase, which functions in the synthesis of carotenoids, from cyanobacteria as a probe to isolate the cDNA for that gene from tomato [Pecker, et al., 1992]. Brief Summary of the Invention In one aspect the present invention provides an isolated and purified polynucleotide of from about 1350 to about 40,000 base pairs that encodes a polypeptide having the ability to catalyze the carboxylation of a biotin carboxyl carrier protein of a cyanobacterium. Preferably, that polypeptide is a subunit of acetyl-CoA carboxylase and participates in the carboxylation of acetyl-CoA. In a preferred embodiment, a cyanobacterium is Anabaena or Synechococcus. The biotin carboxyl carrier protein preferably includes the amino acid residue sequence shown in SEQ ID NO. l l l or a functional equivalent thereof. In another preferred embodiment, the polypeptide has the amino acid residue sequence of Figure 1 or Figure 2. The polynucleotide preferably includes the DNA sequence of SEQ ID NO: l, the DNA sequence of SEQ ID NO: 1 from about nucleotide position 1300 to about nucleotide position 2650 or the DNA sequence of SEQ ID NO:5. In another aspect, the present invention provides an isolated and purified polynucleotide of from about 480 to about 40,000 base pairs that encodes a biotin carboxyl carrier protein of a cyanobacterium and, preferably Anabaena. The biotin carboxyl carrier protein preferably includes the amino acid residue sequence of SEQ ID NO: 111 and the polynucleotide preferably includes the DNA sequence of SEQ ID NO: 110. Another polynucleotide provided by the present invention encodes a plant polypeptide having the ability to catalyze the carboxylation of acetyl-CoA. A plant polypeptide is preferably (1) a monocotyledonous plant polypeptide such as a wheat, rice, maize, barley, rye, oats or timothy grass polypeptide or (2) a dicotyledonous plant polypeptide such as a soybean, rape, sunflower, tobacco, Arabiodopsis, petunia, Canola, pea, bean, tomato, potato, lettuce, spinach, alfalfa, cotton or carrot polypeptide. Preferably, that polypeptide is a subunit of ACC and participates in the carboxylation of acetyl-CoA. Such a polynucleotide preferably includes the nucleotide sequence of SEQ ID NO: 108 and encodes the amino acid residue sequence of SEQ ID NO: 109. In yet another aspect, the present invention provides an isolated and purified DNA molecule comprising a promoter operatively linked to a coding region that encodes (1) a polypeptide having the ability to catalyze the carboxylation of a biotin carboxyl carrier protein of a cyanobacterium, (2) a biotin carboxyl carrier protein of a cyanobacterium or (3) a plant polypeptide having the ability to catalyze the carboxylation of acetyl-CoA, which coding region is operatively linked to a transcription- terminating region, whereby said promoter drives the transcription of said coding region. In another aspect, the present invention provides an isolated polypeptide having the ability to catalyze the carboxylation of a biotin carboxyl carrier protein of a cyanobacterium such as Anabaena or Synechococcus. Preferably a biotin carboxyl carrier protein includes the amino acid sequence of SEQ ID NO: 111 and the polypeptide has the amino acid residue sequence of Figure 1 or Figure 2. The present invention also provides (1) an isolated and purified biotin carboxyl carrier protein of a cyanobacterium such as Anabaena, which protein includes the amino acid residue sequence of SEQ ID NO: 111 and (2) an isolated and purified plant polypeptide having a molecular weight of about 220 kD, dimers of which have the ability to catalyze the carboxylation of acetyl-CoA. In yet another aspect, the present invention provides a process of increasing the herbicide resistance of a monocotyledonous plant comprising transforming the plant with a DNA molecule comprising a promoter operatively linked to a coding region that encodes a herbicide resistant polypeptide having the ability to catalyze the carboxylation of acetyl-CoA, which coding region is operatively linked to a transcription- terminating region, whereby the promoter is capable of driving the transcription of the coding region in a monocotyledonous plant. Preferably, a polypeptide is an acetyl-CoA carboxylase enzyme and, more preferably, a dicotyledonous plant acetyl-CoA carboxylase. In a prefened embodiment, a coding region includes the DNA sequence of SEQ ID NO: 108 and a promoter is CaMV35. The present invention also provides a transformed plant produced in accordance with the above process as well as a transgenic plant and a transgenic plant seed having incorporated into its genome a transgene that encodes a herbicide resistant polypeptide having the ability to catalyze the carboxylation of acetyl-CoA. In yet another aspect, the present invention provides a process of altering the carboxylation of acetyl-CoA in a cell comprising transforming the cell with a DNA molecule comprising a promoter operatively linked to a coding region that encodes a plant polypeptide having the ability to catalyze the carboxylation of acetyl-CoA, which coding region is operatively linked to a transcription-terminating region, whereby the promoter is capable of driving the transcription of the coding region in the cell. In a prefened embodiment, a cell is a cyanobacterium or a plant cell and a plant polypeptide is a monocotyledonous plant acetyl-CoA carboxylase enzyme such as wheat acetyl-CoA carboxylase enzyme. The present invention also provides a transformed cyanobacterium produced in accordance with such a process. The present invention still further provides a process for determining the inheritance of plant resistance to herbicides of the aryloxyphenocypropionate or cyclohexanedione class, which process comprises the steps of: (a) measuring resistance to herbicides of the aryloxyphenocypropionate or cyclohexanedione class in a parental plant line and in progeny of the parental plant line; (b) purifying DNA from said parental plant line and the progeny; (c) digesting the DNA with restriction enzymes to form DNA fragments; (d) fractionating the fragments on a gel; (e) transferring the fragments to a filter support; (f) annealing the fragments with a labelled RFLP probe consisting of a DNA molecule that encodes acetyl-CoA carboxylase or a portion thereof; and (g) detecting the presence of complexes between the fragments and the RFLP probe; and (h) correlating the herbicide resistance of step (a) with the complexes of step (g) and thereby the inheritance of herbicide resistance. Preferably, the acetyl-CoA carboxylase is a dicotyledonous plant acetyl-CoA carboxylase enzyme or a mutated monocotyledonous plant acetyl-CoA carboxylase that confers herbicide resistance or a hybrid acetyl- CoA carboxylase comprising a portion of a dicotyledonous plant acetyl-CoA carboxylase, a portion of a dicotyledonous plant acetyl-CoA carboxylase or one or more domains of a cyanobacterial acetyl-CoA carboxylase. In still yet another aspect, the present invention provides a process for identifying herbicide resistant variants of a plant acetyl-CoA carboxylase comprising the steps of: (a) transforming cyanobacteria with a DNA molecule that encodes a monocotyledonous plant acetyl-CoA carboxylase enzyme to form transformed cyanobacteria; (b) inactivating cyanobacterial acetyl-CoA carboxylase; (c) exposing the transformed cyanobacteria to a herbicide that inhibits acetyl-CoA carboxylase activity; (d) identifying transformed cyanobacteria that are resistant to the herbicide; and (e) characterizing DNA that encodes acetyl-CoA carboxylase from the cyanobacteria of step (d). Brief Description of the Drawings In the drawings which form a portion of the specification: Figure 1 shows the complete nucleotide sequence of a Hindlll fragment that includes the fabG gene coding biotin carboxylase from the cyanobacterium Anabaena 7120, along with the amino acid sequence deduced from the coding sequence of the DNA. Figure 2 shows the nucleotide sequence of the coding region of the fabG gene from the cyanobacterium Anacystis nidulans R2, along with the amino acid sequence deduced from the coding sequence of the DNA. Figure 3 shows an alignment of the amino acid sequences of the BC proteins from both cyanobacteria and from E. coli, the BCCP proteins from Anabaena and from E. coli, along with the ACC enzymes from rat and chicken and several other biotin-con taining carboxylases. Stars indicate positions that are identical in all sequences or all but one. The conventional one letter abbreviations for amino acids are used. The BC domains are indicated by a solid underline, the BCCP domains by a dashed underline. The symbol # indicates sequences not related to BC and, therefore, not considered in the alignment. The wheat ACC sequence deduced from the sequence of our cloned cDNA fragment is on the top line. Abbreviations used in the Figure are: Wh ACC, wheat ACC; Rt, rat; Ch, chicken; Yt, yeast; Sy ACC, Synechococcus BC; An ACC, Anabaena BC and BCCP proteins; EC ACC, E. coli BC and BCCP; Hm PCCA, human propionyl CoA carboxylase; Rt PCCA, rat propionyl CoA carboxylase; Yt PC, yeast pyruvate carboxylase. Figure 4 shows the conserved amino acid sequences used to design primers for the PCR to amplify the BC domain of ACC from wheat. The sequences of the oligonucleotide primers are also shown. In this and other figures showing primer sequences, A means adenine, C means cytosine, G means guanine, T means thymine, N means all four nucleotides, Y means T or C, R means A or G, K means G or T, M means A or C, W means A or T, and H means A,C or T. Figure 5 shows the sequences of the oligonucleotides used as primers for the PCR used to amplify the region of wheat ACC cDNA between the BC and BCCP domains. Figure 6 shows the nucleotide sequence of a portion of the wheat cDNA corresponding to ACC. The amino acid sequence deduced from the nucleotide sequence is also shown. The underlined sequences conespond to the primer sites shown in Figure 5. A unique sequence was found for the BC domain, suggesting that a single mRNA was the template for the final amplified products. For the sequence between the BC and BCCP domains, three different variants were found among four products sequenced, suggesting that three different gene transcripts were among the amplified products. This is not unexpected because wheat is hexaploid, i.e. it has three pairs of each chromosome. Figure 7 shows the sequences of the oligonucleotides used as primers to amplify most of the fabE gene encoding the biotin carboxyl carrier protein from DNA of Anabaena. Figure 8 shows the nucleotide sequence of a PCR product conesponding to a portion of the fabE gene encoding about 75 % of the biotin carboxyl carrier protein from the cyanobacterium Anabaena, along with the amino acid sequence deduced from the coding sequence. The underlined sequences correspond to the primer sites shown in Figure 7. Detailed Description of the Invention I. Definitions The following words and phrases have the meanings set forth below. Expression: The combination of intracellular processes, including transcription and translation undergone by a coding DNA molecule such as a structural gene to produce a polypeptide. Promoter: A recognition site on a DNA sequence or group of DNA sequences that provide an expression control element for a structural gene and to which RNA polymerase specifically binds and initiates RNA synthesis (transcription) of that gene. Regeneration: The process of growing a plant from a plant cell (e.g. plant protoplast or explant). Structural gene: A gene that is expressed to produce a polypeptide. Transformation: A process of introducing an exogenous DNA sequence (e.g. a vector, a recombinant DNA molecule) into a cell or protoplast in which that exogenous DNA is incorporated into a chromosome or is capable of autonomous replication. Transformed cell: A cell whose DNA has been altered by the introduction of an exogenous DNA molecule into that cell. Transgenic cell: Any cell derived or regenerated from a transformed cell or derived from a transgenic cell. Exemplary transgenic cells include plant calli derived from a transformed plant cell and particular cells such as leaf, root, stem, e.g. somatic cells, or reproductive (germ) cells obtained from a transgenic plant. Transgenic plant: A plant or progeny thereof derived from a transformed plant cell or protoplast, wherein the plant DNA contains an introduced exogenous DNA molecule not originally present in a native, non- transgenic plant of the same strain. The terms "transgenic plant" and "transformed plant" have sometimes been used in the art as synonymous terms to define a plant whose DNA contains an exogenous DNA molecule. However, it is thought more scientifically correct to refer to a regenerated plant or callus obtained from a transformed plant cell or protoplast as being a transgenic plant, and that usage will be followed herein. Vector: A DNA molecule capable of replication in a host cell and/or to which another DNA segment can be operatively linked so as to bring about replication of the attached segment. A plasmid is an exemplary vector. Certain polypeptides are disclosed herein as amino acid residue sequences. Those sequences are written left to right in the direction from the amino to the carboxy terminus. In accordance with standard nomenclature, amino acid residue sequences are denominated by either a single letter or a three letter code as indicated below. The present invention provides polynucleotides and polypeptides relating to a whole or a portion of acetyl-CoA carboxylase (ACC) of cyanobacteria and plants as well as processes using those polynucleotides and polypeptides. II. Polynucleotides As used herein the term "polynucleotide" means a sequence of nucleotides connected by phosphodiester linkages. A polynucleotide of the present invention can comprise from about 2 to about several hundred thousand base pairs. Preferably, a polynucleotide comprises from about 5 to about 150,000 base pairs. Prefened lengths of particular polynucleotides are set hereinafter. A polynucleotide of the present invention can be a deoxyribonucleic acid (DNA) molecule or a ribonucleic acid (RNA) molecule. Where a polynucleotide is a DNA molecule, that molecule can be a gene or a cDNA molecule. Nucleotide bases are indicated herein by a single letter code: adenine (A), guanine (G), thymine (T), cytosine (C), and uracil (U). A. Cyanobacteria In one embodiment, the present invention contemplates an isolated and purified polynucleotide of from about 1350 to about 40,000 base pairs that encodes a polypeptide having the ability to catalyze the carboxylation of a biotin carboxyl carrier protein of a cyanobacterium. Preferably, a biotin carboxyl carrier protein (BCCP) is derived from a cyanobacterium such as Anabaena or Synechococcus. A prefened Anabaena is Anabaena 7120. A prefened Synechococcus is Anacystis nidulans R2 (Synechococcus sp. strain pcc7942). A biotin carboxyl carrier protein preferably includes the amino acid residue sequence shown in SEQ ID NO: 111 or a functional equivalent thereof. Preferably, a polypeptide is a biotin carboxylase enzyme of a cyanobacterium, which enzyme is a subunit of acetyl-CoA carboxylase and participates in the carboxylation of acetyl-CoA. In a preferred embodiment, a polypeptide encoded by such a polynucleotide has the amino acid residue sequence of Figure 1 or Figure 2, or a functional equivalent of those sequences. A polynucleotide preferably includes the DNA sequence of SEQ ID NO: l (Figure 1) or the DNA sequence of SEQ ID NO: l (Figure 1) from about nucleotide position 1300 to about nucleotide position 2650. The polynucleotide of SEQ ID NO: 1 contains a gene that encodes the enzyme biotin carboxylase (BC) enzyme from the cyanobacterium Anabaena. This gene was cloned in the following way: total DNA from Anabaena was digested with various restriction enzymes, fractionated by gel electrophoresis, and blotted onto GeneScreen Plus (DuPont). The blot was hybridized at low stringency (1 M NaCl, 57° C.) with a probe consisting of a Sstll-PstI fragment containing about 90% of the coding region of the fabG gene from E. coli. This probe identified a 3.1-kb Hindlll fragment in the Anabaena digest that contained similar sequences. A mixture of about 3-kb Hindlll fragments of Anabaena DNA was purified, then digested with Nhel, yielding a Hindlll-Nhel fragment of 1.6 kb that hybridized with the fabG probe. The 1.6-kb region was purified by gel electrophoresis and cloned into pUC18. Plasmid minipreps were made from about 160 colonies, of which four were found to contain the 1.6-kb Hindlll-Nhel fragment that hybridized with the fabG probe. The 1.6-kb Anabaena fragment was then used as probe to screen, at high stringency (1 M NaCl, 65° C), a cosmid library of Anabaena DNA inserts averaging 40 kb in size. Five were found among 1920 tested, all of which contained the same size Hindlll and Nhel fragments as those identified by the E. coli probe previously. From one of the cosmids, the 3.1-kb Hindlll fragment containing the Anabaena fabG gene was subcloned into pUC18 and sequenced using the dideoxy chain termination method. The complete nucleotide sequence of this fragment is shown in Figure 1. A similar procedure was used to clone the fabG gene from Synechococcus. In this case, the initial Southern hybridization showed that the desired sequences were contained in part on an 0.8-kb BamHI-PstI fragment. This size fragment was purified in two steps and cloned into the plasmid Bluescript KS. Minipreps of plasmids from 200 colonies revealed two that contained the appropriate fragment of Synechococcus DNA. This fragment was used to probe, at high stringency, a library of Synechococcus inserts in the cosmid vector pWB79. One positive clone was found among 1728 tested. This cosmid contained a 2-kb BamHI and a 3-kb PstI fragment that had previously been identified by the E. coli fabG probe in digests of total Synechococcus DNA. Both fragments were subcloned from the cosmid into Bluescript KS and 2.4 kb, including the coding part of the fabG gene, were sequenced. The complete sequence of the coding region of the Synechococcus fabG gene is shown in Figure 2. In another aspect, the present invention provides an isolated and purified polynucleotide of from about 480 to about 40,000 base pairs that encodes a biotin carboxyl carrier protein of a cyanobacterium. That biotin carboxyl carrier protein preferably includes the amino acid residue sequence of Figure 8 (SEQ ID NO: 111) or a functional equivalent thereof. A prefened polynucleotide that encodes that polypeptide includes the DNA sequence of SEQ ID NO: 110 (Figure 8). B. Plants Another polynucleotide contemplated by the present invention encodes a plant polypeptide having the ability to catalyze the carboxylation of acetyl-CoA. Such a plant polypeptide is preferably a monocotyledonous or a dicotyledonous plant acetyl-CoA carboxylase enzyme. An exemplary and prefened monocotyledonous plant is wheat, rice, maize, barley, rye, oats or timothy grass. An exemplary and preferred dicotyledonous plant is soybean, rape, sunflower, tobacco, Arabidopsis, petunia, pea, Canola, bean, tomato, potato, lettuce, spinach, alfalfa, cotton or canot. A monocotyledonous plant polypeptide is preferably wheat ACC, which ACC includes the amino acid residue sequence of SEQ ID NO: 109 (Figure 6) or a functional equivalent thereof. A prefened polynucleotide that encodes such a polypeptide includes the DNA sequence of SEQ ID NO: 108 (Figure 6). Amino acid sequences of biotin carboxylase (BC) from Anabaena and Synechococcus show great similarity with amino acid residue sequences from other ACC enzymes as well as with the amino acid residue sequences of other biotin-containing enzymes (See Figure 3). Based on that homology, the nucleotide sequences shown in Figure 4 were chosen for the construction of primers for polymerase chain reaction amplification of a corresponding region of the gene for ACC from wheat. Those primers have the nucleotide sequences shown below: Primer 1 5' TCGAATTCGTNATNATHAARGC 3' (SEQ ID NO: 112); Primer 2 5' GCTCTAGAGKRTGYTCNACYTG 3' (SEQ ID NO: 113); where N is A, C, G or T; H is A, C or T; R is A or G; Y is T or C and K is G or T. Primers 1 and 2 comprise a 14-nucleotide specific sequence based on a conserved amino acid sequence and an 8-nucleotide extension at the 5'-end of the primer to provide anchors for rounds of amplification after the first round and to provide convenient restriction sites for analysis and cloning. cDNA amplification began with a preparation of total polyA- containing mRNA from eight day-old green plants (Triticum aestivum var. Era as described in [Lamppa, et al., 1992]). The first strand of cDNA was synthesized using random hexamers as primers for AMV reverse transcriptase following procedures described in [Haymerle, et al., 1986], with some modifications. Reverse transcriptase was inactivated by heat and low molecular weight material was removed by filtration. The PCR was initiated by the addition of polymerase at 95°C. Amplification was for 45 cycles, each 1 min at 95°, 1 min at 42-46° and 2 min at 72° C. Both the reactions using Anabaena DNA and the single- stranded wheat cDNA as template yielded about 440 base pair (bp) products. The wheat product was eluted from a gel and reamplified using the same primers. That product, also 440 bp, was cloned into the Invitrogen (San Diego, CA) vector pCRlOOO using their A/T tail method, and sequenced. In eukaryotic ACCs, a BCCP domain is located about 300 amino acids away from the end of the BC domain, on the C-terminal side. Therefore, it is possible to amplify the cDNA covering the interval between the BC and BCCP domains using primers from the C-terminal end of the BC domain and the conserved MKM region of the BCCP. The BC primer was based on the wheat cDNA sequence obtained as described above. Those primers, each with 6- or 8-base 5 '-extensions, are shown below and in Figure 5. Primer 3 5' GCTCTAGAATACTATTTCCTG 3' (SEQ ID NO: 114) Primer 4 5' TCGAATTCWNCATYTTCATNRC 3' (SEQ ID NO: 115) N, R and Y are as defined above. W is A or T. The BC primer (Primer 3) was based on the wheat cDNA sequence obtained as described above. The MKM primer (primer 4) was first checked by determining whether it would amplify the fabE gene coding BCCP from Anabaena DNA. This PCR was primed at the other end by using a primer based on the N-terminal amino acid residue sequence as determined on protein purified from Anabaena extracts by affinity chromatography. Those primers are shown below and in Figure 7. Primer 5 5' GCTCTAGAYTTYAAYGARATHMG 3' (SEQ ID NO: 116) Primer 4 5' TCGAATTCWNCATYTTCATNRC 3' (SEQ ID NO: 115) H, N, R, T, Y and W are as defined above. M is A or C. This amplification (using the conditions described above) yielded the conect fragment of the Anabaena fabE gene, which was used to identify cosmids that contained the entire fabE gene and flanking DNA. An about 4 kb Xbal fragment containing the gene was cloned into the vector Bluescript KS for sequencing. Primers 3 and 4 were then used to amplify the intervening sequence in wheat cDNA. Again, the product of the first PCR was eluted and reamplified by another round of PCR, then cloned into the Invitrogen vector pCRII. The complete 1.1 kb of the amplified DNA was sequenced, shown in Figure 6, nucleotides 376-1473. The nucleotide sequence of the BC domain is also shown in Figure 6, nucleotides 1-422. Three clones of the BC domain gave the sequence shown. Four clones of the 1.1 -kb fragment differed at several positions, conesponding to three closely related sequences, all of which are indicated in the Figure. Most of the sequence differences are in the third codon position and are silent in terms of the amino acid sequence. The amino acid sequence of the polypeptide predicted from the cDNA sequence for this entire fragment of wheat cDNA (1473 nucleotides) is compared with the amino acid sequences of other ACC enzymes and related enzymes from various sources in Figure 3. The most significant identities are with the ACC of rat, chicken and yeast, as shown in the table below. Less extensive similarities are evident with the BC subunits of bacteria and the BC domains of other enzymes such as pyruvate carboxylase of yeast and propionyl CoA carboxylase of rat. The amino acid identities between wheat ACC and other biotin-dependent enzymes, within the BC domain (amino acid residues 312-630 in Figure 3) are shown below in Table 1. Table 1 yeast pyruvate carboxylase 31 C. Probes and Primers In another aspect, DNA sequence information provided by the invention allows for the preparation of relatively short DNA (or RNA) sequences having the ability to specifically hybridize to gene sequences of the selected polynucleotides disclosed herein. In these aspects, nucleic acid probes of an appropriate length are prepared based on a consideration of a selected ACC gene sequence, e.g., a sequence such as that shown in Figures 1, 2, 6 or 8. The ability of such nucleic acid probes to specifically hybridize to an ACC gene sequence lend them particular utility in a variety of embodiments. Most importantly, the probes can be used in a variety of assays for detecting the presence of complementary sequences in a given sample. In certain embodiments, it is advantageous to use oligonucleotide primers. The sequence of such primers is designed using a polynucleotide of the present invention for use in detecting, amplifying or mutating a defined segment of an ACC gene from a cyanobacterium or a plant using PCR technology. Segments of ACC genes from other organisms can also be amplified by PCR using such primers. To provide certain of the advantages in accordance with the present invention, a prefened nucleic acid sequence employed for hybridization studies or assays includes sequences that are complementary to at least a 10 to 30 or so long nucleotide stretch of an ACC sequence, such as that shown in Figures 1, 2, 6 or 8. A size of at least 10 nucleotides in length helps to ensure that the fragment will be of sufficient length to form a duplex molecule that is both stable and selective. Molecules having complementary sequences over stretches greater than 10 bases in length are generally prefened, though, in order to increase stability and selectivity of the hybrid, and thereby improve the quality and degree of specific hybrid molecules obtained. One will generally prefer to design nucleic acid molecules having gene-complementary stretches of 15 to 20 nucleotides, or even longer where desired. Such fragments may be readily prepared by, for example, directly synthesizing the fragment by chemical means, by application of nucleic acid reproduction technology, such as the PCR technology of U.S. Patent 4,603, 102, herein incorporated by reference, or by excising selected DNA fragments from recombinant plasmids containing appropriate inserts and suitable restriction sites. Accordingly, a nucleotide sequence of the invention can be used for its ability to selectively form duplex molecules with complementary stretches of the gene. Depending on the application envisioned, one will desire to employ varying conditions of hybridization to achieve varying degree of selectivity of the probe toward the target sequence. For applications requiring a high degree of selectivity, one will typically desire to employ relatively stringent conditions to form the hybrids, for example, one will select relatively low salt and .or high temperature conditions, such as provided by 0.02M-0.15M NaCl at temperatures of 50°C to 70°C. These conditions are particularly selective, and tolerate little, if any, mismatch between the probe and the template or target strand. Of course, for some applications, for example, where one desires to prepare mutants employing a mutant primer strand hybridized to an underlying template or where one seeks to isolate an ACC coding sequences for related species, functional equivalents, or the like, less stringent hybridization conditions will typically be needed in order to allow formation of the heteroduplex. In these circumstances, one may desire to employ conditions such as 0.15M-0.9M salt, at temperatures ranging from 20 °C to 55 °C. Cross-hybridizing species can thereby be readily identified as positively hybridizing signals with respect to control hybridizations. In any case, it is generally appreciated that conditions can be rendered more stringent by the addition of increasing amounts of formamide, which serves to destabilize the hybrid duplex in the same manner as increased temperature. Thus, hybridization conditions can be readily manipulated, and thus will generally be a method of choice depending on the desired results. In certain embodiments, it is advantageous to employ a polynucleotide of the present invention in combination with an appropriate label for detecting hybrid formation. A wide variety of appropriate labels are known in the art, including radioactive, enzymatic or other ligands, such as avidin/biotin, which are capable of giving a detectable signal. In general, it is envisioned that a hybridization probe described herein is useful both as a reagent in solution hybridization as well as in embodiments employing a solid phase. In embodiments involving a solid phase, the test DNA (or RNA) is adsorbed or otherwise affixed to a selected matrix or surface. This fixed nucleic acid is then subjected to specific hybridization with selected probes under desired conditions. The selected conditions depend as is well known in the art on the particular circumstances and criteria required (e.g., on the G+C contents, type of target nucleic acid, source of nucleic acid, size of hybridization probe). Following washing of the matrix to remove nonspecifically bound probe molecules, specific hybridization is detected, or even quantified, by means of the label. D. Expression Vector The present invention contemplates an expression vector comprising a polynucleotide of the present invention, Thus, in one embodiment an expression vector is an isolated and purified DNA molecule comprising a promoter operatively linked to an coding region that encodes a polypeptide having the ability to catalyze the carboxylation of a biotin carboxyl carrier protein of a cyanobacterium, which coding region is operatively linked to a transcription-terminating region, whereby the promoter drives the transcription of the coding region. As used herein, the term "operatively linked" means that a promoter is connected to an coding region in such a way that the transcription of that coding region is controlled and regulated by that promoter. Means for operatively linking a promoter to a coding region are well known in the art. Where an expression vector of the present invention is to be used to transform a cyanobacterium, a promoter is selected that has the ability to drive and regulate expression in cyanobacteria. Promoters that function in bacteria are well known in the art. An exemplary and preferred promoter for the cyanobacterium Anabaena is the glnA gene promoter. An exemplary and prefened promoter for the cyanobacterium Synechococcus is the psbAI gene promoter. Alternatively, the cyanobacterial fabG gene promoters themselves can be used. Where an expression vector of the present invention is to be used to transform a plant, a promoter is selected that has the ability to drive expression in plants. Promoters that function in plants are also well known in the art. Useful in expressing the polypeptide in plants are promoters that are inducible, viral, synthetic, constitutive as described by Poszkowski et al., EMBO J.. 3:2719 (1989) and Odell et al., Nature. 313:810 (1985), and temporally regulated, spatially regulated, and spatiotemporally regulated as given in Chau et al., Science. 244: 174-181 (1989). A promoter is also selected for its ability to direct the transformed plant cell's or transgenic plant's transcriptional activity to the coding region. Structural genes can be driven by a variety of promoters in plant tissues. Promoters can be near-constitutive, such as the CaMV 35S promoter, or tissue specific or developmentally specific promoters affecting dicots or monocots. Where the promoter is a near-constitutive promoter such as CaMV 35S. increases in polypeptide expression are found in a variety of transformed plant tissues (e.g. callus, leaf, seed and root). Alternatively, the effects of transformation can be directed to specific plant tissues by using plant integrating vectors containing a tissue-specific promoter. An exemplary tissue-specific promoter is the Lectin promoter, which is specific for seed tissue. The Lectin protein in soybean seeds is encoded by a single gene (Lei) that is only expressed during seed maturation and accounts for about 2 to about 5 percent of total seed mRNA. The Lectin gene and seed-specific promoter have been fully characterized and used to direct seed specific expression in transgenic tobacco plants. See, e.g.. Vodkin et al., Cejl, 34:1023 (1983) and Lindstrom et al., Developmental Genetics. 11 : 160 (1990). An expression vector containing a coding region that encodes a polypeptide of interest is engineered to be under control of the Lectin promoter and that vector is introduced into plants using, for example, a protoplast transformation method. Dhir et al., Plant Cell Reports. 10:97 (1991). The expression of the polypeptide is directed specifically to the seeds of the transgenic plant. A transgenic plant of the present invention produced from a plant cell transformed with a tissue specific promoter can be crossed with a second transgenic plant developed from a plant cell transformed with a different tissue specific promoter to produce a hybrid transgenic plant that shows the effects of transformation in more than one specific tissue. Exemplary tissue-specific promoters are corn sucrose synthetase 1 (Yang et al. Proc. Natl. Acad. Sci. U.S.A.. 87:4144-48 (1990)), corn alcohol dehydrogenase 1 (Vogel et al., J. Cell Biochem.. (supplement 13D, 312) (1989)), corn zein 19KD gene (storage protein) (Boston et al., Plant Physiol.. 83:742-46), corn light harvesting complex (Simpson, Science. 233:34 (1986), corn heat shock protein (O'Dell et al., Nature. 313:810-12 (1985), pea small subunit RuBP Carboxylase (Poulsen et al., Mol. Gen. Genet.. 205: 193-200 (1986); Cashmore et al. , Gen. Eng. of Plants. Plenum Press, New York, 29-38 (1983), Ti plasmid mannopine synthase (Langridge et al., Proc. Natl. Acad. Sci. USA. 86:3219-3223 (1989), Ti plasmid nopaline synthase (Langridge et al., Proc. Natl. Acad. Sci. USA. 86:3219-3223 (1989), petunia chalcone isomerase (Van Tunen et al., EMBO J.. 7: 1257 (1988), bean glycine rich protein 1 (Keller et al., EMBO J.. 8: 1309-14 (1989), CaMV 35s transcript (O'Dell et al., Nature. 313:810-12 (1985) and Potato patatin (Wenzler et al., Plant Mol. Biol.. 12:41-50 (1989). Prefened promoters are the cauliflower mosaic virus (CaMV 35S) promoter and the S-E9 small subunit RuBP carboxylase promoter. The choice of which expression vector and ultimately to which promoter a polypeptide coding region is operatively linked depends directly on the functional properties desired, e.g. the location and timing of protein expression, and the host cell to be transformed. These are well known limitations inherent in the art of constructing recombinant DNA molecules. However, a vector useful in practicing the present invention is capable of directing the expression of the polypeptide coding region to which it is operatively linked. Typical vectors useful for expression of genes in higher plants are well known in the art and include vectors derived from the tumor- inducing (Ti) plasmid of Agrobacterium tumefaciens described by Rogers et al., Meth. in Enzvmol.. 153:253-277 (1987). However, several other plant integrating vector systems are known to function in plants including pCaMVCN transfer control vector described by Fromm et al., Proc. Natl. Acad. Sci. USA. 82:5824 (1985). Plasmid pCaMVCN (available from Pharmacia, Piscataway, NJ) includes the cauliflower mosaic virus CaMV 35S promoter. In prefened embodiments, the vector used to express the polypeptide includes a selection marker that is effective in a plant cell, preferably a drug resistance selection marker. One prefened drug resistance marker is the gene whose expression results in kanamycin resistance; i.e., the chimeric gene containing the nopaline synthase promoter, Tn5 neomycin phosphotransferase II and nopaline synthase 3' nontranslated region described by Rogers et al., in Methods For Plant Molecular Biology. A. Weissbach and H. Weissbach, eds., Academic Press Inc., San Diego, CA (1988). RNA polymerase transcribes a coding DNA sequence through a site where polyadenylation occurs. Typically, DNA sequences located a few hundred base pairs downstream of the polyadenylation site serve to terminate transcription. Those DNA sequences are refened to herein as transcription-termination regions. Those regions are required for efficient polyadenylation of transcribed messenger RNA (mRNA). Means for preparing expression vectors are well known in the art. Expression (transformation vectors) used to transform plants and methods of making those vectors are described in United States Patent Nos. 4,971,908, 4,940,8354,769,061 and 4,757,011, the disclosures of which are incorporated herein by reference. Those vectors can be modified to include a coding sequence in accordance with the present invention. A variety of methods has been developed to operatively link DNA to vectors via complementary cohesive termini or blunt ends. For instance, complementary homopolymer tracts can be added to the DNA segment to be inserted and to the vector DNA. The vector and DNA segment are then joined by hydrogen bonding between the complementary homopolymeric tails to form recombinant DNA molecules. A coding region that encodes a polypeptide having the ability to catalyze the carboxylation of a biotin carboxyl carrier protein of a cyanobacterium is preferably a biotin carboxylase enzyme of a cyanobacterium, which enzyme is a subunit of acetyl-CoA carboxylase and participates in the carboxylation of acetyl-CoA. In a prefened embodiment, such a polypeptide has the amino acid residue sequence of Figure 1 or Figure 2, or a functional equivalent of those sequences. In accordance with such an enbodiment, a coding region comprises the entire DNA sequence of SEQ ID NO: l (Figure 1) or the DNA sequence of SEQ ID NO: l (Figure 1) from about nucleotide position 1300 to about nucleotide position 2650 or the DNA sequence of SEQ ID NO:5 (Figure 2). In another embodiment, an expression vector comprises a coding region of from about 480 to about 40,000 base pairs that encodes a biotin carboxyl carrier protein of a cyanobacterium. That biotin carboxyl carrier protein preferably includes the amino acid residue sequence of Figure 8 (SEQ ID NO: 111) or a functional equivalent thereof. A prefened such coding region includes the DNA sequence of SEQ ID NO: 110 (Figure 8). In still yet another embodiment, an expression vector comprises a coding region that encodes a plant polypeptide having the ability to catalyze the carboxylation of acetyl-CoA. Such a plant polypeptide is preferably a monocotyledonous or a dicotyledonous plant acetyl-CoA carboxylase enzyme. A prefened monocotyledonous plant polypeptide encoded by such a coding region is preferably wheat ACC, which ACC includes the amino acid residue sequence of SEQ ID NO: 109 (Figure 6) or a functional equivalent thereof. A prefened coding region includes the DNA sequence of SEQ ID NO: 108 (Figure 6). HL Polypeptide The present invention contemplates a polypeptide that defines a whole or a portion of an ACC of a cyanobacterium or a plant. In one embodiment, thus, the present invention provides an isolated polypeptide having the ability to catalyze the carboxylation of a biotin carboxyl carrier protein of a cyanobacterium such as Anabaena or Synechococcus. Preferably, a biotin carboxyl carrier protein includes the amino acid sequence of SEQ ID NO: l l l and the polypeptide has Figure 1 or Figure 2. The present invention also contemplates an isolated and purified biotin carboxyl carrier protein of a cyanobacterium such as Anabaena, which protein includes the amino acid residue sequence of SEQ ID NO: l l l. In another embodiment, the present invention contemplates an isolated and purified plant polypeptide having a molecular weight of about 220 KD, dimers of which have the ability to catalyze the carboxylation of acetyl-CoA. Such a polypeptide preferably includes the amino acid residue sequence of SEQ ID NO: 109. Modification and changes may be made in the structure of polypeptides of the present invention and still obtain a molecule having like or otherwise desirable characteristics. For example, certain amino acids may be substituted for other amino acids in a protein structure without appreciable loss of interactive binding capacity with structures such as, for example, antigen-binding regions of antibodies or binding sites on substrate molecules. Since it is the interactive capacity and nature of a polypeptide that defines that polypeptide 's biological functional activity, certain amino acid sequence substitutions can be made in a polypeptide sequence (or, of course, its underlying DNA coding sequence) and nevertheless obtain a polypeptide with like or even counterveiling properties (e.g., antagonistic v. agonistic). In making such changes, the hydropathic index of amino acids may be considered. The importance of the hydropathic amino acid index in conferring interactive biologic function on a protein is generally understood in the art (Kyte & Doolittle, J. Mol. Biol., 157: 105-132, 1982). It is known that certain amino acids may be substituted for other amino acids having a similar hydropathic index or score and still result in a protein with similar biological activity. Each amino acid has been assigned a hydropathic index on the basis of their hydrophobicity and charge characteristsics, these are: isoleucine (+4.5); valine (+4.2); leucine (+3.8); phenylalanine (+2.8); cysteine/cystine (+2.5); methionine (+ 1.9); alanine (+ 1.8); glycine (-0.4); threonine (-0.7); serine (-0.8); tryptophan (-0.9); tyrosine (-1.3); proline (-1.6); histidine (-3.2); glutamate (-3.5); glutamine (-3.5); aspartate (-3.5); asparagine (-3.5); lysine (-3.9); and arginine (-4.5). It is believed that the relative hydropathic character of the amino acid determines the secondary structure of the resultant polypeptide, which in turn defines the interaction of the polypeptide with other molecules, for example, enzymes, substrates, receptors, antibodies, antigens, and the like. It is known in the art that an amino acid may be substituted by another amino acid having a similar hydropathic index and still obtain a biological functionally equivalent protein. In such changes, the substitution of amino acids whose hydropathic indices are within ±2 is prefened, those which are within + 1 are particularly prefened, and those within +0.5 are even more particularly prefened. Substitution of like amino acids can also be made on the basis of hydrophilicity, particularly where the biological functional equivalent protein or peptide thereby created is intended for use in immunological embodiments. U.S. Patent 4,554, 101, incorporated herein by reference, states that the greatest local average hydrophilicity of a protein, as governed by the hydrophilicity of its adjacent amino acids, conelates with its immunogenicity and antigenicity, i.e. with a biological property of the protein. As detailed in U.S. Patent 4,554,101, the following hydrophilicity values have been asssigned to amino acid residues: arginine (+3.0); lysine (+3.0); aspartate (+3.0 ± 1); glutamate (+3.0 ± 1); serine (+0.3); asparagine (+0.2); glutamine (+0.2); glycine (0); proline (-0.5 + 1); threonine (-0.4); alanine (-0.5); histidine (-0.5); cysteine (-1.0); methionine (-1.3); valine (-1.5); leucine (-1.8); isoleucine (-1.8); tyrosine (-2.3); phenylalanine (-2.5); tryptophan (-3.4). It is understood that an amino acid can be substituted for another having a similar hydrophilicity value and still obtain a biologically equivalent, and in particular, an immunologically equivalent protein. In such changes, the substitution of amino acids whose hydrophilicity values are within +2 is prefened, those which are within + 1 are particularly prefened, and those within +0.5 are even more particularly prefened. As outlined above, amino acid substitutions are generally therefore based on the relative similarity of the amino acid side-chain substituents, for example, their hydrophobicity, hydrophilicity, charge, size, and the like. Exemplary substitutions which take various of the foregoing characteristics into consideration are well known to those of skill in the art and include: arginine and lysine; glutamate and aspartate; serine and threonine; glutamine and asparagine; and valine, leucine and isoleucine. The present invention thus contemplates functional equivalents of the polypeptides set forth above. A polypeptide of the present invention is prepared by standard techniques well known to those skilled in the art. Such techniques include, but are not limited to, isolation and purification from tissues known to contain that polypeptide and expression from cloned DNA using transformed cells. IV. Transformed or transgenic cells or plants A cyanobacterium, a plant cell or a plant transformed with an expression vector of the present invention is also contemplated. A transgenic cyanobacterium, plant cell or plant derived from such a transformed or transgenic cell is also contemplated. Means for transforming cyanobacteria are well known in the art. Typically, means of transformation are similar to those well known means used to transform other bacteria such as E. coli. Synechococcus can be transformed simply by incubation of log-phase cells with DNA. (Golden, et al., 1987) The application of brief, high-voltage electric pulses to a variety of mammalian and plant cells leads to the formation of nanometer- sized pores in the plasma membrane. DNA is taken directly into the cell cytoplasm either through these pores or as a consequence of the redistribution of membrane components that accompanies closure of the pores. Electroporation can be extremely efficient and can be used both for transient expression of clones genes and for establishment of cell lines that carry integrated copies of the gene of interest. Electroporation, in contrast to calcium phosphate-mediated transfection and protoplast fusion, frequently gives rise to cell lines that carry one, or at most a few, integrated copies of the foreign DNA. Methods for DNA transformation of plant cells include Agrobacterium-mediated plant transformation, protoplast transformation, gene transfer into pollen, injection into reproductive organs, injection into immature embryos and particle bombardment. Each of these methods has distinct advantages and disadvantages. Thus, one particular method of introducing genes into a particular plant strain may not necessarily be the most effective for another plant strain, but it is well known which methods are useful for a particular plant strain. Agrobacterium-mediated transfer is a widely applicable system for introducing genes into plant cells because the DNA can be introduced into whole plant tissues, thereby bypassing the need for regeneration of an intact plant from a protoplast. The use of Agrobacterium-mediated plant integrating vectors to introduce DNA into plant cells is well known in the art. See, for example, the methods described by Fraley et al., Biotechnology. 3:629 (1985) and Rogers et al.. Methods in Enzymology. 153:253-277 (1987). Further, the integration of the Ti-DNA is a relatively precise process resulting in few rearrangements. The region of DNA to be transfened is defined by the border sequences, and intervening DNA is usually inserted into the plant genome as described by Spielmann et al., Mol. Gen. Genet.. 205:34 (1986) and Jorgensen et al., Mol. Gen. Genet.. 207:471 (1987). Modern Agrobαcterium transformation vectors are capable of replication in E. coli as well as Agrobαcterium, allowing for convenient manipulations as described by Klee et al., in Plant DNA Infectious Agents. T. Hohn and J. Schell, eds., Springer- Verlag, New York (1985) pp. 179- 203. Moreover, recent technological advances in vectors for Agrobacterium-mediated gene transfer have improved the arrangement of genes and restriction sites in the vectors to facilitate construction of vectors capable of expressing various polypeptide coding genes. The vectors described by Rogers et al., Methods in Enzymology. 153:253 (1987), have convenient multi-linker regions flanked by a promoter and a polyadenylation site for direct expression of inserted polypeptide coding genes and are suitable for present purposes. In addition, Agrobacteria containing both armed and disarmed Ti genes can be used for the transformations. In those plant strains where Agrobacterium-mediated transformation is efficient, it is the method of choice because of the facile and defined nature of the gene transfer. Agrobacterium-mediated transformation of leaf disks and other tissues such as cotyledons and hypocotyls appears to be limited to plants that Agrobαcterium naturally infects. Agrobacterium-mediated transformation is most efficient in dicotyledonous plants. Few monocots appear to be natural hosts for Agrobαcterium, although transgenic plants have been produced in asparagus using Agrobαcterium vectors as described by Bytebier et al. , Proc. Natl. Acad. Sci. USA. 84:5345 (1987). Therefore, commercially important cereal grains such as rice, corn, and wheat must usually be transformed using alternative methods. However, as mentioned above, the transformation of asparagus using Agrobαcterium can also be achieved. See, for example, Bytebier, et al., Proc. Natl. Acad. Sci. USA. 84:5345 (1987). A transgenic plant formed using Agrobαcterium transformation methods typically contains a single gene on one chromosome. Such transgenic plants can be refened to as being heterozygous for the added gene. However, inasmuch as use of the word "heterozygous" usually implies the presence of a complementary gene at the same locus of the second chromosome of a pair of chromosomes, and there is no such gene in a plant containing one added gene as here, it is believed that a more accurate name for such a plant is an independent segregant, because the added, exogenous gene segregates independently during mitosis and meiosis. More prefened is a transgenic plant that is homozygous for the added structural gene; i.e. , a transgenic plant that contains two added genes, one gene at the same locus on each chromosome of a chromosome pair. A homozygous transgenic plant can be obtained by sexually mating (selfing) an independent segregant transgenic plant that contains a single added gene, germinating some of the seed produced and analyzing the resulting plants produced for enhanced carboxylase activity relative to a control (native, non-transgenic) or an independent segregant transgenic plant. It is to be understood that two different transgenic plants can also be mated to produce offspring that contain two independently segregating added, exogenous genes. Selfing of appropriate progeny can produce plants that are homozygous for both added, exogenous genes that encode a polypeptide of interest. Back-crossing to a parental plant and out- crossing with a non-transgenic plant are also contemplated. Transformation of plant protoplasts can be achieved using methods based on calcium phosphate precipitation, polyethylene glycol treatment, electroporation, and combinations of these treatments. See, for example, Potrykus et al., Mol. Gen. Genet.. 199: 183 (1985); Lorz et al., Mol. Gen. Genet.. 199: 178 (1985); Fromm et al., Nature. 319:791 (1986); Uchimiya et al., Mol. Gen. Genet.. 204:204 (1986); Callis et al., Genes and Development. 1:1183 (1987); and Marcotte et al., Nature. 335:454 (1988). Application of these systems to different plant strains depends upon the ability to regenerate that particular plant strain from protoplasts. Illustrative methods for the regeneration of cereals from protoplasts are described in Fujimura et al., Plant Tissue Culture Letters. 2:74 (1985); Toriyama et al., Theor Appl. Genet.. 73: 16 (1986); Yamada et al., Plant Cell Rep.. 4:85 (1986); Abdullah et al., Biotechnology. 4: 1087 (1986). To transform plant strains that cannot be successfully regenerated from protoplasts, other ways to introduce DNA into intact cells or tissues can be utilized. For example, regeneration of cereals from immature embryos or explants can be effected as described by Vasil, Biotechnology. 6:397 (1988). In addition, "particle gun" or high-velocity microprojectile technology can be utilized. (Vasil, 1992) Using that latter technology, DNA is carried through the cell wall and into the cytoplasm on the surface of small metal particles as described in Klein et al., Nature. 327:70 (1987); Klein et al., Proc. Natl. Acad. Sci. U.S.A.. 85:8502 (1988); and McCabe et al., Biotechnology. 6:923 (1988). The metal particles penetrate through several layers of cells and thus allow the transformation of cells within tissue explants. Metal particles have been used to successfully transform corn cells and to produce fertile, stable transgenic tobacco plants as described by Gordon-Kamm, W.J. et al., The Plant Cell. 2:603-618 (1990); Klein, T.M. et al., Plant Phvsiol.. 91:440-444 (1989); Klein, T.M. et al., Proc. Natl. Acad. Sci. USA. 85:8502-8505 (1988); and Tomes, D.T. et al., Plant Mol. Biol.. 14:261-268 (1990). Transformation of tissue explants eliminates the need for passage through a protoplast stage and thus speeds the production of transgenic plants. Thus, the amount of a gene coding for a polypeptide of interest (i.e., a polypeptide having carboxylation activity) can be increased in monocotyledonous plants such as corn by transforming those plants using particle bombardment methods. Maddock et al., Third International Congress of Plant Molecular Biology. Abstract 372 (1991). By way of example, an expression vector containing an coding region for a dicotyledonous ACC and an appropriate selectable marker is transformed into a suspension of embryonic maize (corn) cells using a particle gun to deliver the DNA coated on microprojectiles. Transgenic plants are regenerated from transformed embryonic calli that express ACC. Particle bombardment has been used to successfully transform wheat (Vasil et al., 1992). DNA can also be introduced into plants by direct DNA transfer into pollen as described by Zhou et al., Methods in Enzymology. 101:433 (1983); D. Hess, Intern Rev. Cytol.. 107:367 (1987); Luo et al., Plant Mol. Biol. Reporter. 6: 165 (1988). Expression of polypeptide coding genes can be obtained by injection of the DNA into reproductive organs of a plant as described by Pena et al., Nature. 325:274 (1987). DNA can also be injected directly into the cells of immature embryos and the rehydration of desiccated embryos as described by Neuhaus et al., Theor. Appl. Genet.. 75:30 (1987); and Benbrook et al., in Proceedings Bio Expo 1986. Butterworth, Stoneham, MA, pp. 27-54 (1986). The development or regeneration of plants from either single plant protoplasts or various explants is well known in the art. See, for example, Methods for Plant Molecular Biology. A. Weissbach and H. Weissbach, eds., Academic Press, Inc., San Diego, CA (1988). This regeneration and growth process typically includes the steps of selection of transformed cells, culturing those individualized cells through the usual stages of embryonic development through the rooted plantlet stage. Transgenic embryos and seeds are similarly regenerated. The resulting transgenic rooted shoots are thereafter planted in an appropriate plant growth medium such as soil. The development or regeneration of plants containing the foreign, exogenous gene that encodes a polypeptide of interest introduced by Agrobacterium from leaf explants can be achieved by methods well known in the art such as described by Horsch et al., Science. 227: 1229-1231 (1985). In this procedure, transformants are cultured in the presence of a selection agent and in a medium that induces the regeneration of shoots in the plant strain being transformed as described by Fraley et al., Proc. Natl. Acad. Sci. U.S.A.. 80:4803 (1983). This procedure typically produces shoots within two to four months and those shoots are then transfened to an appropriate root-inducing medium containing the selective agent and an antibiotic to prevent bacterial growth. Shoots that rooted in the presence of the selective agent to form plantlets are then transplanted to soil or other media to allow the production of roots. These procedures vary depending upon the particular plant strain employed, such variations being well known in the art. Preferably, the regenerated plants are self-pollinated to provide homozygous transgenic plants, as discussed before. Otherwise, pollen obtained from the regenerated plants is crossed to seed-grown plants of agronomically important, preferably inbred lines. Conversely, pollen from plants of those important lines is used to pollinate regenerated plants. A transgenic plant of the present invention containing a desired polypeptide is cultivated using methods well known to one skilled in the art. Any of the transgenic plants of the present invention can be cultivated to isolate the desired ACC or fatty acids which are the products of the series of reactions of which that catalyzed by ACC is the first. A transgenic plant of this invention thus has an increased amount of an coding region (e.g. gene) that encodes a polypeptide of interest. A prefened transgenic plant is an independent segregant and can transmit that gene and its activity to its progeny. A more prefened transgenic plant is homozygous for that gene, and transmits that gene to all of its offspring on sexual mating. Seed from a transgenic plant is grown in the field or greenhouse, and resulting sexually mature transgenic plants are self- pollinated to generate true breeding plants. The progeny from these plants become true breeding lines that are evaluated for, by way of example, herbicide resistance, preferably in the field, under a range of environmental conditions. The commercial value of a transgenic plant with increased herbicide resistance or with altered fatty acid production is enhanced if many different hybrid combinations are available for sale. The user typically grows more than one kind of hybrid based on such differences as time to maturity, standability or other agronomic traits. Additionally, hybrids adapted to one part of a country are not necessarily adapted to another part because of differences in such traits as maturity, disease and herbicide resistance. Because of this, herbicide resistance is preferably bred into a large number of parental lines so that many hybrid combinations can be produced. V. Process of increasing herbicide resistance Herbicides such as aryloxyphenoxypropionates and cyclohexanediones inhibit the growth of monocotyledonous weeds by interfering with fatty acid biosynthesis of herbicide sensitive plants. ACC is the target enzyme for those herbicides. Dicotyledonous plants, other eukaryotic organisms and prokaryotic organisms are resistant to those compounds. Thus, the resistance of sensitive monocotyledonous plants to herbicides can be increased by providing those plants with ACC that is not sensitive to herbicide inhibition. The present invention therefore provides a process of increasing the herbicide resistance of a monocotyledonous plant comprising transforming the plant with a DNA molecule comprising a promoter operatively linked to a coding region that encodes a herbicide resistant polypeptide having the ability to catalyze the carboxylation of acetyl-CoA, which coding region is operatively linked to a transcription- terminating region, whereby the promoter is capable of driving the transcription of the coding region in a monocotyledonous plant. Preferably, a herbicide resistant polypeptide, a dicotyledonous plant polypeptide such as an acetyl-CoA carboxylase enzyme from soybean, rape, sunflower, tobacco, Arabidopsis, petunia, Canola, pea, bean, tomato, potato, lettuce, spinach, alfalfa, cotton or canot, or functional equivalent thereof. A promoter and a transcription-terminating region are preferably the same as set forth above. Transformed monocotyledonous plants can be identified using herbicide resistance. A process for identifying a transformed monocotyledonous plant cell comprises the steps of: (a) transforming the monocotyledonous plant cell with a DNA molecule that encodes a dicotyledonous acetyl-CoA carboxylase enzyme; and (b) determining the resistance of the plant cell to a herbicide and thereby the identification of the transformed monocotyledonous plant cell. Means for transforming a monocotyledonous plant cell are the same as set forth above. The resistance of a transformed plant cell to a herbicide is preferably determined by exposing such a cell to an effective herbicidal dose of a preselected herbicide and maintaining that cell for a period of time and under culture conditions sufficient for the herbicide to inhibit ACC, alter fatty acid biosynthesis or retard growth. The effects of the herbicide can be studied by measuring plant cell ACC activity, fatty acid synthesis or growth. An effective herbicidal dose of a given herbicide is that amount of the herbicide that retards growth or kills plant cells not containing herbicide-resistant ACC or that amount of a herbicide known to inhibit plant growth. Means for determining an effective herbicidal dose of a given herbicide are well known in the art. Preferably, a herbicide used in such a process is an aryloxyphenoxypropionate or cyclohexanedione herbicide. VI. Process of altering ACC activity Acetyl-CoA carboxyase catalyzes the carboxylation of acetyl- CoA. Thus, the carboxylation of acetyl-CoA in a cyanobacterium or a plant can be altered by, for example, increasing an ACC gene copy number or changing the composition (e.g., nucleotide sequence) of an ACC gene. Changes in ACC gene composition can alter gene expression at either the transcriptional or translational level. Alternatively, changes in gene composition can alter ACC function (e.g., activity, binding) by changing primary, secondary or tertiary structure of the enzyme. By way of example, certain changes in ACC structure are associated with changes in the resistance of that altered ACC to herbicides. The copy number of such a gene can be increased by transforming a cyanobacterium or a plant cell with an appropriate expression vector comprising a DNA molecule that encodes ACC. In one embodiment, therefore, the present invention contemplates a process of altering the carboxylation of acetyl-CoA in a cell comprising transforming the cell with a DNA molecule comprising a promoter operatively linked to a coding region that encodes a polypeptide having the ability to catalyze the carboxylation of acetyl-CoA, which coding region is operatively linked to a transcription-terminating region, whereby the promoter is capable of driving the transcription of the coding region in the cyanobacterium. In a prefened embodiment, a cell is a cyanobacterium or a plant cell, a polypeptide is a cyanobacterial ACC or a plant ACC. Exemplary and prefened expression vectors for use in such a process are the same as set forth above. Where a cyanobacterium is transformed with a plant ACC DNA molecule, that cyanobacterium can be used to identify herbicide resistant mutations in the gene encoding ACC. In accordance with such a use, the present invention provides a process for identifying herbicide resistant variants of a plant acetyl-CoA carboxylase comprising the steps of: (a) transforming cyanobacteria with a DNA molecule that encodes a monocotyledonous plant acetyl-CoA carboxylase enzyme to form transformed or transfected cyanobacteria; (b) inactivating cyanobacterial acetyl-CoA carboxylase; (c) exposing the transformed cyanobacteria to an effective herbicidal amount of a herbicide that inhibits acetyl-CoA carboxylase activity; (d) identifying transformed cyanobacteria that are resistant to the herbicide; and (e) characterizing DNA that encodes acetyl-CoA carboxylase from the cyanobacteria of step (d). Means for transforming cyanobacteria as well as expression vectors used for such transformation are preferably the same as set forth above. In a prefened embodiment, cyanobacteria are transformed or transfected with an expression vector comprising an coding region that encodes wheat ACC. Cyanobacteria resistant to the herbicide are identified. Identifying comprises growing or culturing transformed cells in the presence of the herbicide and recovering those cells that survive herbicide exposure. Transformed, herbicide-resistant cells are then grown in culture, collected and total DNA extracted using standard techniques. ACC DNA is isolated, amplified if needed and then characterized by comparing that DNA with DNA from ACC known to be inhibited by that herbicide. VII. Process for Determining Herbicide Resistance Inheritibility In yet another aspect, the present invention provides a process for determining the inheritance of plant resistance to herbicides of the aryloxyphenocypropionate or cyclohexanedione class. That process comprises the steps of: (a) measuring resistance to herbicides of the aryloxyphenocypropionate or cyclohexanedione class in a parental plant line and in progeny of the parental plant line to; (b) purifying DNA from the parental plant line and the progeny; (c) digesting the DNA with restriction enzymes to form DNA fragments; (d) fractionating the fragments on a gel; (e) transferring the fragments to a filter support; (f) annealing the fragments with a labelled RFLP probe consisting of a DNA molecule that encodes acetyl-CoA carboxylase or a portion thereof; (g) detecting the presence of complexes between the fragments and the RFLP probe; and (h) conelating the herbicide resistance of step (a) with the complexes of step (g) and thereby the inheritance of herbicide resistance. In a prefened embodiment, the herbicide resistant variant of acetyl-CoA carboxylase is a dicotyledonous plant acetyl-CoA carboxylase enzyme or a portion thereof. In another prefened embodiment, the herbicide resistant variant of acetyl-CoA carboxylase is a mutated monocotyledonous plant acetyl-CoA carboxylase that confers herbicide resistance or a hybrid acetyl-CoA carboxylase comprising a portion of a dicotyledonous plant acetyl-CoA carboxylase, a portion of a dicotyledonous plant acetyl-CoA carboxylase or one or more domains of a cyanobacterial acetyl-CoA carboxylase. The inheritability of phenotypic traits such as herbicide resistance can be determined using RFLP analysis. Restriction fragment length polymorphisms (RFLPs) are due to sequence differences detectable by lengths of DNA fragments generated by digestion with restriction enzymes and typically revealed by agarose gel electrophoresis. There are large numbers of restriction endonucleases available, characterized by their recognition sequences and source. Restriction fragment length polymorphism analyses are conducted, for example, by Native Plants Incorporated (NPI). This service is available to the public on a contractual basis. For this analysis, the genetic marker profile of the parental inbred lines is determined. If parental lines are essentially homozygous at all relevant loci (i.e., they should have only one allele at each locus), the diploid genetic marker profile of the hybrid offspring of the inbred parents should be the sum of those parents, e.g., if one parent had the allele A at a particular locus, and the other parent had B, the hybrid AB is by inference. Probes capable of hybridizing to specific DNA segments under appropriate conditions are prepared using standard techniques well known to those skilled in the art. The probes are labelled with radioactive isotopes or fluorescent dyes for ease of detection. After restriction fragments are separated by size, they are identified by hybridization to the probe. Hybridization with a unique cloned sequence permits the identification of a specific chromosomal region (locus). Because all alleles at a locus are detectable, RFLP's are co-dominant alleles, thereby satisfying a criteria for a genetic marker. They differ from some other types of markers, e.g., from isozymes, in that they reflect the primary DNA sequence, they are not products of transcription or translation. Furthermore, different RFLP profiles result from different anays of restriction endonucleases. The foregoing examples illustrate particular embodiments of the present invention. It will be readily apparent to a skilled artisan that changes, modification and alterations can be made to those embodiments without departing from the true scope or spirit of the invention. Example 1: Isolation of Cyanobacterial ACC Polynucleotides The polynucleotide of SEQ ID NO: 1 contains a gene that encodes the enzyme biotin carboxylase (BC) enzyme from the cyanobacterium Anabaena 7120. This gene was cloned from a total DNA extract of Anabaena that was digested with various restriction enzymes, fractionated by gel electrophoresis, and blotted onto GeneScreen Plus (DuPont). The blot was hybridized at low stringency (1 M NaCl, 57° C.)with a probe consisting of a Sstll-PstI fragment containing about 90% of the coding region of the fabG gene from E. coli. This probe identified a 3.1-kb Hindlll fragment in the Anabaena digest that contained similar sequences. A mixture of about 3-kb Hindlll fragments of Anabaena DNA was purified, then digested with Nhel, yielding a Hindlll-Nhel fragment of 1.6 kb that hybridized with the fabG probe. The 1.6-kb region was purified by gel electrophoresis and cloned into pUC18. Plasmid minipreps were made from about 160 colonies, of which four were found to contain the 1.6- kb Hindlll-Nhel fragment that hybridized with the fabG probe. The 1.6-kb Anabaena fragment was then used as probe to screen, at high stringency (1 M NaCl, 65° C), a cosmid library of Anabaena DNA inserts averaging 40 kb in size. Five were found among 1920 tested, all of which contained the same size Hindlll and Nhel fragments as those identified by the E. coli probe previously. From one of the cosmids, the 3.1-kb Hindlll fragment containing the Anabaena fabG gene was subcloned into pUC18 and sequenced using the dideoxy chain termination method. The complete nucleotide sequence of this fragment is shown in Figure 1. A similar procedure was used to clone the fabG gene from Synechococcus. In this case, the initial Southern hybridization showed that the desired sequences were contained in part on an 0.8-kb BamHI-PstI fragment. This size fragment was purified in two steps and cloned into the plasmid Bluescript KS. Minipreps of plasmids from 200 colonies revealed two that contained the appropriate fragment of Synechococcus DNA. This fragment was used to probe, at high stringency, a library of Synechococcus inserts in the cosmid vector pWB79. One positive clone was found among 1728 tested. This cosmid contained a 2-kb BamHI and a 3-kb PstI fragment that had previously been identified by the E. coli fabG probe in digests of total Synechococcus DNA. Both fragments were subcloned from the cosmid into Bluescript KS and 2.4 kb, including the coding part of the fabG gene, were sequenced. The complete sequence of the coding region of the Anacystis fabG gene is shown in Figure 2. Example 2: Plant ACC The amino acid sequences of the fabG genes encoding BC from Anabaena and Synechococcus are aligned with sequences of ACC and other biotin-containing enzymes from several sources in Figure 3. This comparison allows the designation of several areas of significant conservation among all the proteins, indicated by stars in the Figure. Based on this alignment, the sequences shown in Figure 4 were chosen for the construction of primers for the polymerase chain reaction, in order to amplify the conesponding region of the gene for ACC from wheat. The primers used for this amplification are shown in Figure 4. Each consists of a 14-nucleotide specific sequence based on the amino acid sequence and an 8-nucleotide extension at the 5 '-end of the primer to provide anchors for rounds of amplification after the first round and to provide convenient restriction sites for future analysis and cloning. cDNA amplification began with a preparation of total polyA- containing mRNA from eight day-old green plants (Triticum αestivum var. Era as described in [Lamppa, et al., 1992]). The first strand of cDNA was synthesized using random hexamers as primers for AMV reverse transcriptase following procedures described in [Haymerle, et al., 1986], with some modifications. Reverse transcriptase was inactivated by incubation at 90° C and low molecular weight material was removed by filtration through centricon 100. All components of the PCR (from the Cetus/Perkin-Elmer kit) together with the two primers shown in Figure 4, except the Taq DNA polymerase, were incubated for 3-5 min at 95° C. The PCR was initiated by the addition of polymerase. Conditions were established and optimized using Anabaena DNA as template, in order to provide the best yield and lowest level of non-specific products for amplification of the target BC gene from Anabaena DNA. Amplification was for 45 cycles, each 1 min at 95°, 1 min at 42-46° and 2 min at 72° C. Both the reactions using Anabaena DNA and the single-stranded wheat cDNA as template yielded about 440-bp products. The wheat product was eluted from a gel and reamplified using the same primers. That product, also 440 bp, was cloned into the Invitrogen vector pCRlOOO using their A/T tail method, and sequenced. The nucleotide sequence is shown in Figure 5. In eukaryotic ACCs, the BCCP domain is located about 300 amino acids away from the end of the BC domain, on the C-terminal side. Therefore, it is possible to amplify the cDNA covering that interval using primers from the C-terminal end of the BC domain and the conserved MKM region of the BCCP. The BC primer was based on the wheat cDNA sequence obtained as described above. These primers, each with 6- or 8- base 5 '-extensions, are shown in Figure 6B. The MKM primer was first checked by determing whether it would amplify the fabE gene encoding BCCP from Anabaena DNA. This PCR was primed at the other end by using a primer based on the N-terminal amino acid sequence, determined on protein purified from Anabaena extracts by affinity chromatography, shown in Figure 6A. This amplification (using the conditions described above) worked, yielding the conect fragment of the Anabaena fabE gene, whose complete sequence is shown in Figure 7. The PCR-amplified fragment of the Anabaena fabE gene was used to identify cosmids (three detected in a library of 1920) that contain the entire fabE gene and flanking DNA. A 4-kb Xbal fragment containing the gene was cloned into the vector Bluescript KS for sequencing. The two primers shown in Figure 6 were then used to amplify the intervening sequence in wheat cDNA. Again, the product of the first PCR was eluted and reamplified by another round of PCR, then cloned into the Invitrogen vector pCRII. The complete 1.1 kb of the amplified DNA was sequenced, also shown in Figure 5. The foregoing examples illustrate particular embodiments of the present invention. One of ordinary skill in the art will readily appreciate that changes, modifications and alterations to those embodiments can be made without departing from the true scope or spirit of the invention. References The references listed below and all references cited herein are incorporated herein by reference to the extent that they supplement, explain, provide a background for, or teach methodology, techniques, and/or compositions employed herein. 1. J.R.Knowles. 1989. The mechanism of biotin-dependent enzymes. Annu. Rev. Biochem. 58: 195-221. 2. Alix, J.-H. 1989. A rapid procedure for cloning genes from I libraries by complementation of E. coli defective mutants: application to the fabE region of the E. coli chromosome. DNA 8: 779-789. 3. Muramatsu, S., and T. Mizuno. 1989. Nucleotide sequence of the fabE gene and flanking regions containing a bent DNA sequence of Escherichia coli. Nucleic Acids Res. 17: 3982. 4. Li, S., and J. E. Cronan. 1992. The gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase. J. Biol. Chem. 267: 855. 5. Lopez-Casillas, F., D. H. Bai, X. Luo, I. S. Kong, M. A. Hermodson, and K. H. Kim. 1988. Structure of the coding sequence and primary amino acid sequence of rat Acetyl- coenzyme A carboxylase. Proc. Natl. Acad. Sci. USA 85: 5784-5788. 6. Takai, T., C. Yokoyama, K. Wada, and T. Tanabe. 1988. Primary structure of chicken liver acetyl-coenzyme A carboxylase deduced from cDNA sequence. J. Biol. Che . : 2651-2657. 6a. W. A. Feel, S. S. Chirala and S. J. Wakil 1992. Cloning of the yeast FAS3 gene and primary structure of yeast acetyl-CoA carboxylase. Proc Natl Acad, Sci USA 89: 4534-4538. 7. J.L.Harwood. 1988. Fatty acid metabolism. Ann. Rev. Physiol. Plant Mol. Biol. 39: 101-138. 8. Egin-Buhler, B., and J. Ebel. 1983. Improved purification and further characterization of ACC from culture cells of parsley. Eur. J. Bioche . 133: 335-339. 9. Wurtele,E.S. and Nikolau,B.J. 1990. Arch. Biochem. Biophys. 278: 179-186. 10. Slabas,A.R. and Hellyer,A. 1985. Plant Sci. 39: 177-182. 11. Samols, D., C. G. Thornton, V. L. Murtif, G. K. Kumar, F. C. Haase, and H. G. Wood. 1988. Evolutionary conservation among biotin enzymes. J. Biol. Chem. 263: 6461-6464. 12. H.K.Lichtenthaler. 1990. Mode of action of herbicides affecting acetyl-CoA carboxylase and fatty acid biosynthesis. Z. Naturforsch. 45c: 521-528. 13. I. Pecker, D. Chamovitz, H. Linden, G. Sandmann and J. Hirschberg. 1992. A single polypeptide catalyzing the conversion of phytoene to z-carotene is transcriptionally regulated during tomato fruit ripening. Proc Natl Acad Sci USA 89: 4962-4666. 14. G. K. Lamppa, G. Morelli and N-H Chua (1985). Structure and developmental regulation of a wheat gene encoding the major chlorophyll a/b-binding polypeptide. Mol. Cell Biol. 5: 1370-1378. 15. H. Haymerle, J. Herz, G. M. Bressan, R. Frank and K. K. Stanley (1986). Efficient construction of cDNA libraries in plasmid expression vectors using an adaptor strategy. Nucl. Acids Res. 14: 8615-8629. 16. V. Vasil, A. M. Castillo, M. E. Fromm and I. K. Vasil (1992). Herbicide-resistant fertile transgenic wheat plants obtained by microprojectile bombardment of regenerable embryogenic callus. Biotechnology 10: 667-674. 17. S. S. Golden, T. Brusslen and R. Haselkorn (1987), Genetic Enginerring of the Cyanobacterial Chromosome. Methods Enzy ology 153: 215-231. SEQUENCE LISTING: (1) GENERAL INFORMATION: (i) Applicants: Robert Haselkorn and Piotr Gornicki (ϋ) Title of Invention: Cyanobacterial and Plant Acetyl-CoA Carboxylase (iii) Number of Sequences: 116 (iv) Correspondence Address: (v) Computer Readable Form: (A) Medium Type: Floppy Disk (B) Computer: IBM PC Compatible (C) Operating System: PC-DOS/MS-DOS (D) Software: ASCII-DOS (vi) Current Application Data: (A) Application Number: 07/956,700 (B) Filing Date: 10/21/92 (C) Classification: Unknown (vii) Attorney/Agent Information: (A) Name: Thomas E. Northrup (B) Registration Number: 33,268 (C) Reference/Docket Number: ARCD:058 (viii) Telecommunication Information: (A) Telephone: 1-312-744-0090 (B) Telefax: 1-312-755-4489 (2) INFORMATION FOR SEQ ID Nθ:l: (i) Sequence characteristics: (A) Length: 3065 base pairs (B) Type: Nucleic acid (C) strandedness: Single (D) Topology: Linear (ii) Molecule Type: Oligonucleotide (xi) Sequence Description: SEQ ID NO:l: AAGCTTTTAT ATTTTGCCAT TTCTAGAACT TAGCTGCATC GGCCCCAAGT ATTTTGTCAA 60 ATATGGCGAA AAGACTTCAT AAATCAAGGT TAAAGGTTGA CCGTGATGCC AAAACAGGTA 120 ATGGCGACCC CAGAAAGGCC CATCCACGCC AAAACCTAAT TGCAAGGCCT CTGAATTTCC 180 GTAATAAATA CCCCGCACAT CCCGATACAA CTCCGTGCGA AGACGAGCTA GACTTGCCCA 240 AATTGGTAAT GAACGGTTTT GCAAATACTC GTCTACATGG CTGGCTTCCC ACCATGAGGT 300 TGCATAGGCG AGTCGTTGGC CAGAGCGTGT ACGTAGCCAT ACCTGTCGCC GCAGTCTTGG 360 CGCTGGAACA GATTGGATTA AATCCGGCGC ACTATCTAAA TCCAAACCAA TCAATGACAT 420 ATCAATGACA TCGACTTCTG TTGGCTCACC AGTAAGTAAT TCTAAATGCC TTGTGGGTGA 480 GCCATCACCT AAGAGTAGTA GTTGCCACGC TGGAGCCAGC TGAGTGTGAG GCAAACTATG 540 TTTAATTACT TCTTCCCCAC CTTGCCAAAT AGGAGTGAGG CGATGCCATC CGGCTGGCAG 600 TGTTGAGTTG TTGCTTGGAG TAAAAGTGGC AGTCAATGTT CTTTACAAAA GTTCACCTAT 660 TTATATCAAA GCATAAAAAA TTAATTAGTT GTCAGTTGTC ATTGGTTATT CTTCTTTGCT 720 CCCCCTGCCC CCTACTTCCC TCCTCTGCCC AATAATTAGA AAGGTCAGGA GTCAAAAACT 780 TATCACTTTT GACCACTGAC CTTTCACAAT TGACTATAGT CACTAAAAAA TGCGGATGGC 840 GAGACTCGAA CTCGCAAGGC AAAGCCACAC GCACCTCAAG CGTGCGCGTA TACCAATTCC 900 GCCACATCCG CACGGGTTGT ACAAGAAGAT ATACTAGCAC AAAAAAATTG CATAAAACAA 960 GGTAAAACTA TATTTGCCAA ACTTTATGGA AAATTTATCT TGCTAAATAT ACAAATTTCC 1020 CGAAGAGGAT ACGAGACTAA CAGAAATGTA GTATCGCCAC AAGTGATATT AAAGGGGGTA 1080 TGGGGGTTTT CTTCCCTTAC ACCCTTAAAC CCTCACACCC CACCTCCATG AAAAATCTTG 1140 TTGGTAAGTC CGTTTCCTGC AATTTATTTA AAGATGAGCC TGGGGTATCT CCTGTCATAA 1200 TTTGAGATGA AGCGATGCCT AAGGCGGCTA CGCTACGCGC TAAAAGCAAC TTGGATGGGA 1260 GACAATTTCT ATCTGCTGGT ACTGATACTG ATATCGAAAA CTAGAAAATG AAGTTTGACA 1320 AAATATTAAT TGCCAATCGG GGAGAAATAG CGCTGCGCAT TCTCCGCGCC TGTGAGGAAA 1380 TGGGGATTGC GACGATCGCA GTTCATTCGA CTGTTGACCG GAATGCTCTT CATGTCCAAC 1440 TTGCTGACGA AGCGGTTTGT ATTGGCGAAC CTGCTAGCGC TAAAAGTTAT TTGAATATTC 1500 CCAATATTAT TGCTGCGGCT TTAACGCGCA ATGCCAGTGC TATTCATCCT GGGTATGGCT 1560 TTTTATCTGA AAATGCCAAA TTTGCGGAAA TCTGTGCTGA CCATCACATT GCATTCATTG 1620 GCCCCACCCC AGAAGCTATC CGCCTCATGG GGGACAAATC CACTGCCAAG GAAACCATGC 1680 AAAAAGCTGG TGTACCGACA GTACCGGGTA GTGAAGGTTT GGTAGAGACA GAGCAAGAAG 1740 GATTAGAACT GGCGAAAGAT ATTGGCTACC CAGTGATGAT CAAAGCCACG GCTGGTGGTG 1800 GCGGCCGGGG TATGCGACTG GTGCGATCGC CAGATGAATT TGTCAAACTG TTCTTAGCCG 1860 CCCAAGGTGA AGCTGGTGCA GCCTTTGGTA ATGCTGGCGT TTATATAGAA AAATTTATTG 1920 AACGTCCGCG CCACATTGAA TTTCAAATTT TGGCTGATAA TTACGGCAAT GTGATTCACT 1980 TGGGTGAGAG GGATTGCTCA ATTCAGCGTC GTAACCAAAA GTTACTAGAA GAAGCCCCCA 2040 GCCCAGCCTT GGACTCAGAC CTAAGGGAAA AAATGGGACA AGCGGCGGTG AAAGCGGCTC 2100 AGTTTATCAA TTACGCCGGG GCAGGTACTA TCGAGTTTTT GCTAGATAGA TCCGGTCAGT 2160 TTTACTTTAT GGAGATGAAC ACCCGGATTC AAGTAGAACA TCCCGTAACT GAGATGGTTA 2220 CTGGAGTGGA TTTATTGGTT GAGCAAATCA GAATTGCCCA AGGGGAAAGA CTTAGACTAA 2280 CTCAAGACCA AGTAGTTTTA CGCGGTCATG CGATCGAATG TCGCATCAAT GCCGAAGACC 2340 CAGACCACGA TTTCCGCCCA GCACCCGGAC GCATTAGCGG TTATCTTCCC CCTGGCGGCC 2400 CTGGCGTGCG GATTGACTCC CACGTTTACA CGGATTACCA AATTCCGCCC TACTACGATT 2460 CCTTAATTGG TAAATTGATC GTTTGGGGCC CTGATCGCGC TACTGCTATT AACCGCATGA 2520 AACGCGCCCT CAGGGAATGC GCCATCACTG GATTACCTAC AACCATTGGG TTTCATCAAA 2580 GAATTATGGA AAATCCCCAA TTTTTACAAG GTAATGTGTC TACTAGTTTT GTGCAGGAGA 2640 TGAATAAATA GGGTAATGGG TAATGGGTAA TGGGTAATAG AGTTTCAATC ACCAATTACC 2700 AATTCCCTAA CTCATCCGTG CCAACATCGT CAGTAATCCT TGCTGGCCTA GAAGAACTTC 2760 TCGCAACAGG CTAAAAATAC CAACACACAC AATGGGGGTG ATATCAACAC CACCTATTGG 2820 TGGGATGATT TTTCGCAAGG GAATGAGAAA TGGTTCAGTC GGCCAAGCAA TTAAGTTGAA 2880 GGGCAAACGG TTCAGATCGA CTTGCGGATA CCAGGTCAGA ATGATACGGA AAATAAACAG 2940 AAATGTCATC ACTCCCAATA CAGGGCCAAG AATCCAAACG CTCAGGTTAA CACCAGTCAT 3000 CGATCTAAGC TACT TTTTG TGAATTTACA AAAAACTGCA AGCAAAAGCT GAAAATTTTA 3060 AGCTT 3065 (2) INFORMATION FOR SEQ ID NO:2: (i) Sequence characteristics: (A) Length: 32 amino acids (B) Type: Amino acid (C) strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:2: Asp Glu Ala Met Pro Lys Ala Ala Thr Leu Arg Ala Lys Ser Asn Leu 5 10 15 Asp Gly Arg Gin Phe Leu Ser Ala Gly Thr Asp Thr Asp lie Glu Asn 20 25 30 (2) INFORMATION FOR SEQ ID NO:3: (i) Sequence characteristics: (A) Length: 427 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:3: Lys Met Lys Phe Asp Lys lie Leu lie Ala Asn Arg Gly Glu lie Ala 5 10 15 Leu Arg lie Leu Arg Ala Cys Glu Glu Met Gly lie Ala Thr lie Ala 20 25 30 Val His Ser Thr Val Asp Arg Asn Ala Leu His Val Gin Leu Ala Asp 35 40 45 Glu Ala Val Cys lie Gly Glu Pro Ala Ser Ala Lys Ser Tyr Leu Asn 50 55 60 lie Pro Asn lie lie Ala Ala Ala Leu Thr Arg Asn Ala Ser Ala lie 65 70 75 80 His Pro Gly Tyr Gly Phe Leu Ser Glu Asn Ala Lys Phe Ala Glu lie 85 90 95 Cys Ala Asp His His lie Ala Phe lie Gly Pro Thr Pro Glu Ala lie 100 105 110 Arg Leu Met Gly Asp Lys Ser Thr Ala Lys Glu Thr Met Gin Lys Ala 115 120 125 Gly Val Pro Thr Val Pro Gly Ser Glu Gly Leu Val Glu Thr Glu Gin 130 135 140 Glu Gly Leu Glu Leu Ala Lys Asp lie Gly Tyr Pro Val Met lie Lys 145 150 155 160 Ala Thr Ala Gly Gly Gly Gly Arg Gly Met Arg Leu Val Arg Ser Pro 165 170 175 Asp Glu Phe Val Lys Leu Phe Leu Ala Ala Gin Gly Glu Ala Gly Ala 180 185 190 Ala Phe Gly Asn Ala Gly Val Tyr lie Glu Lys Phe lie Glu Arg Pro 195 200 205 Arg His lie Glu Phe Gin lie Leu Ala Asp Asn Tyr Gly Asn Val lie 210 215 220 His Leu Glu Arg Asp Cys Ser lie Gin Arg Arg Asn Gin Lys Leu Leu 225 230 235 240 Glu Glu Ala Pro Ser Pro Ala Leu Asp Ser Asp Leu Arg Glu Lys Met 245 250 255 Gly Gin Ala Ala Val Lys Ala Ala Gin Phe lie Asn Tyr Ala Gly Ala 260 265 270 Gly Thr lie Glu Phe Leu Leu Asp Arg Ser Gly Gin Phe Gly Val Asp 275 280 285 Leu Leu Val Glu Gin lie Arg lie Ala Gin Gly Glu Arg Leu Arg Leu 290 295 300 Thr Gin Asp Gin Val Val Leu Arg Gly His Ala lie Glu Cys Arg lie 305 310 315 320 Asn Ala Glu Asp Pro Asp His Asp Phe Arg Pro Ala Pro Gly Arg lie 325 330 335 Ser Gly Tyr Leu Pro Pro Gly Gly Pro Gly Val Arg lie Asp Ser His 340 345 350 Val Tyr Thr Asp Tyr Gin lie Pro Pro Tyr Tyr Asp Ser Leu lie Gly 355 360 365 Lys Leu lie Val Trp Gly Pro Asp Arg Ala Thr Ala lie Asn Arg Met 370 375 380 Lys Arg Ala Leu Arg Glu Cys Ala lie Thr Gly Leu Pro Thr Thr lie 385 390 395 400 Gly Phe His Gin Arg lie Met Glu Asn Pro Gin Phe Leu Gin Gly Asn 405 410 415 Val Ser Thr Ser Phe Val Gin Glu Met Asn Lys 420 425 (2) INFORMATION FOR SEQ ID NO: : (i) Sequence characteristics: (A) Length: 36 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:4: Trp Val Met Gly Asn Arg Val Ser lie Thr Asn Tyr Gin Phe Pro Asn 5 10 15 Ser Ser Val Pro Thr Ser Ser Val lie Leu Ala Gly Leu Glu Glu Leu 20 25 30 Leu Ala Thr Gly 35 (2) INFORMATION FOR SEQ ID NO:5: (i) Sequence characteristics: (A) Length: 1342 base pairs (B) Type: Nucleic acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Oligonucleotide (xi) Sequence Description: SEQ ID NO:5: ATGCGTTTCA ACAAGATCCT GATCGCCAAT CGCGGCGAAA TCGCCCTGCG CATTCTCCGC 60 ACTTGTCAAG AACTCGGGAT CGGCACGATC GCCGTTCACT CCACTGTGGA TCGCAACGCG 120 CTCCATGTGC AGTTAGCGGA CGAAGCGGTC TGTATTGGCG AAGCGGCCAG CAGCAAAAGC 180 TATCTCAATA TCCCCAACAT CATTGCGGCG GCCCTGACCC CTAATGCCAG CGCCATTCAC 240 CCCGGCTATG GCTTCTTGGC GGAGAATGCC CGCTTTGCAG AAATCTGCGC CGATCACCAT 300 CTCACCTTTA TTGGCCCCAG CCCCGATTCG ATTCGAGCCA TGGGCGATAA ATCCACCGCT 360 AAGGAAACAA TGCAGCGGGT CGGCGTTCCG ACGATTCCGG GCAGTGACGG TCTGCTGACG 400 GATGTTGATT CGGCTGCCAA AGTTGCTGCC GAGATCGGCT ATCCCGTCAT GATCAAAGCG 460 ACGGCGGGGG GCGGTGGTCG CGGTATGCGG CTGGTGCGTG ACCCTGCAGA TCTGGAAAAA 520 CTGTTCCTTG CTGCCCAAGG AGAAGCCGAG GCAGCTTTTG GGAATCCAGG ACTGTATCTC 580 GAAAAATTTA TCGATCGCCC ACGCCACGTT GAATTTCAGA TCTTGGCCGA TGCCTACGGC 640 AATGTAGTGC ATCTAGGCGA GCGCGATTGC TCCATTCAAC GTCGTCACCA AAAGCTGCTC 700 GAAGAAGCCC CCAGTCCGGC GCTATCGGCA GACCTGCGGC AGAAAATGGG CGATGCCGCC 760 GTCAAAGTCG CTCAAGCGAT CGGCTACATC GGTGCCGGCA CCGTGGAGTT TCTGGTCGAT 820 GCGACCGGCA ACTTCTACTT CATGGAGATG AATACCCGCA TCCAAGTCGA GCATCCAGTC 900 ACAGAAATGA TTACGGGACT GGACTTGATT GCGGAGCAGA TTCGGATTGC CCAAGGCGAA 960 GCGCTGCGCT TCCGGCAAGC CGATATTCAA CTGCGCGGCC ATGCGATCGA ATGCCGTATC 1020 AATGCGGAAG ATCCGGAATA CAATTTCCGG CCGAATCCTG GCCGCATTAC AGGCTATTTA 1080 CCGCCCGGCG GCCCCGGCGT TCGTGTCGAT TCCCATGTTT ATACCGACTA CGAAATTCCG 1140 CCCTATTACG ATTCGCTGAT TGGCAAATTG ATTGTCTGGG GTGCAACACG GGAAGAGGCG 1200 ATCGCGCGGA TGCAGCGTGC TCTGCGGGAA TGCGCCATCA CCGGCTTGCC GACGACCCTT 1260 AGTTTCCATC AGCTGATGTT GCAGATGCCT GAGTTCCTGC GCGGGGAACT CTATACCAAC 1300 TTTGTTGAGC AGGTGATGCT ACCTCGGATC CTCAAGTCCT AG 1342 (2) INFORMATION FOR SEQ ID NO:6: (i) Sequence characteristics: (A) Length: 453 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:6: Met Arg Phe Asn Lys lie Leu lie Ala Asn Arg Gly Glu lie Ala Leu 5 10 15 Arg lie Leu Arg Thr Cys Glu Glu Leu Gly lie Gly Thr lie Ala Val 20 25 30 His Ser Thr Val Asp Arg Asn Ala Leu His Val Gin Leu Ala Asp Glu 35 40 45 Ala Val Cys lie Gly Glu Ala Ala Ser Ser Lys Ser Tyr Leu Asn lie 50 55 60 Pro Asn lie lie Ala Ala Ala Leu Thr Arg Asn Ala Ser Ala lie His 65 70 75 80 Pro Gly Tyr Gly Phe Leu Ala Glu Asn Ala Arg Phe Ala Glu lie Cys 85 90 95 Ala Asp His His Leu Thr Phe lie Gly Pro Ser Pro Asp Ser lie Arg 100 105 110 Ala Met Gly Asp Lys Ser Thr Ala Lys Glu Thr Met Gin Arg Val Gly 115 120 125 Val Pro Thr lie Pro Gly Ser Asp Gly Leu Leu Thr Asp Val Asp Ser 130 135 140 Ala Ala Lys Val Ala Ala Glu He Gly Tyr Pro Val Met He Lys Ala 145 150 155 160 Thr Ala Gly Gly Gly Gly Arg Gly Met Arg Leu Val Arg Glu Pro Ala 165 170 175 Asp Leu Glu Lys Leu Phe Leu Ala Ala Gin Gly Glu Ala Glu Ala Ala 180 185 190 Phe Gly Asn Pro Gly Leu Tyr Leu Glu Lys Phe He Asp Arg Pro Arg 195 200 205 His Val Glu Phe Gin He Leu Ala Asp Ala Tyr Gly Asn Val Val Glu 210 215 220 Leu Gly Glu Arg Asp Cys Ser He Gin Arg Arg His Gin Lys Leu Leu 225 230 235 240 Glu Glu Ala Pro Ser Pro Ala Leu Ser Ala Asp Leu Arg Gin Lys Met 245 250 255 Gly Asp Ala Ala Val Lys Val Ala Gin Ala He Gly Tyr He Gly Ala 260 265 270 Gly Thr Val Glu Phe Leu Val Asp Ala Thr Gly Asn Phe Tyr Phe Met 275 280 285 Glu Met Asn Thr Arg He Gin Val Glu His Pro Val Thr Glu Met He 290 295 300 Thr Gly Leu Asp Leu He Ala Glu Gin He Arg He Ala Gin Gly Glu 305 310 315 320 Ala Leu Arg Phe Arg Gin Ala Asp He Gin Leu Arg Gly His Ala He 325 330 335 Glu Cys Arg He Asn Ala Glu Asp Pro Glu Tyr Asn Phe Arg Pro Asn 340 345 350 Pro Gly Arg He Thr Gly Tyr Leu Pro Pro Gly Gly Pro Gly Val Arg 355 360 265 Val Asp Ser His Val Tyr Thr Asp Tyr Glu He Pro Pro Tyr Tyr Asp 370 375 380 Ser Leu He Gly Lys Leu He Val Trp Gly Ala Thr Arg Glu Glu Ala 385 390 395 400 He Ala Arg Met Gin Arg Ala Leu Arg Glu Gly Ala He Thr Gly Leu 405 410 415 Pro Thr Thr Leu Ser Phe His Gin Leu Met Leu Gin Met Pro Glu Phe 420 425 430 Leu Arg Gly Glu Leu Tyr Thr Asn Phe Val Glu Gin Val Met Leu Pro 435 440 445 Arg He Leu Lys Ser 450 (2) INFORMATION FOR SEQ ID NO:7: (i) Sequence characteristics: (A) Length: 34 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:7: Met Asp Glu Pro Ser Pro Leu Ala Lys Thr Leu Glu Leu Asn Gin His 5 10 15 Ser Arg Phe He He Gly Ser Val Ser Glu Asp Asn Ser Glu Asp Glu 20 25 30 He Ser (2) INFORMATION FOR SEQ ID NO:8: (i) Sequence characteristics: (A) Length: 187 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:8: Asn Leu Val Lys Leu Asp Leu Glu Glu Lys Glu Gly Ser Leu Ser Pro 5 10 15 Ala Ser Val Ser Ser Asp Thr Leu Ser Asp Leu Gly He Ser Ala Leu 20 25 30 Gin Asp Gly Leu Ala Phe His Met Arg Ser Ser Met Ser Gly Leu His 35 40 45 Leu Val Lys Gin Gly Arg Asp Arg Lys Lys He Asp Ser Gin Arg Asp 50 55 60 Phe Thr Val Ala Ser Pro Ala Glu Phe Val Thr Arg Phe Gly Gly Asn 65 70 75 80 Lys Val He Glu Lys Val Leu He Ala Asn Asn Gly He Ala Ala Val 85 90 95 Lys Cys Met Arg Ser He Arg Arg Trp Ser Tyr Glu Met Phe Arg Asn 100 105 110 Glu Arg Ala He Arg Phe Val Val Met Val Thr Pro Glu Asp Leu Lys 115 120 125 Ala Asn Ala Glu Tyr He Lys Met Ala Asp His Tyr Val Pro Val Pro 130 135 140 Gly Gly Ala Asn Asn Asn Asn Tyr Ala Asn Val Glu Leu He Leu Asp 145 150 155 160 He Ala Lys Arg He Pro Val Gin Ala Val Trp Ala Gly Trp Gly His 165 170 175 Ala Ser Glu Asn Pro Lys Leu Pro Glu Leu Leu 180 185 (2) INFORMATION FOR SEQ ID NO: : (i) Sequence characteristics: (A) Length: 122 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:9: Leu Lys Asn Gly He Ala Phe Met Gly Pro Pro Ser Gin Ala Met Trp 5 10 15 Ala Leu Gly Asp Lys He Ala Ser Ser He Val Ala Gin Thr Ala Gly 20 25 30 He Pro Thr Leu Pro Trp Ser Gly Ser Gly Leu Arg Val Asp Trp Gin 35 40 45 Glu Asn Asp Phe Ser Lys Arg He Leu Asn Val Pro Gin Asp Leu Tyr 40 55 60 Glu Lys Gly Tyr Val Lys Asp Val Asp Asp Gly Leu Lys Ala Ala Glu 65 70 75 80 Glu Val Gly Tyr Pro Val Met He Lys Ala Ser Glu Gly Gly Gly Gly 85 90 95 Lys Gly He Arg Lys Val Asn Asn Ala Asp Asp Phe Pro Asn Leu Phe 100 105 110 Arg Gin Val Gin Ala Glu Val Pro Gly Ser 115 120 (2) INFORMATION FOR SEQ ID NO:10: (i) Sequence characteristics: (A) Length: 86 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:10: Pro He Phe Val Met Arg Leu Ala Lys Gin Ser Arg His Leu Glu Val 5 10 15 Gin He Leu Ala Asp Gin Tyr Gly Asn Ala He Ser Leu Phe Gly Arg 20 25 30 Asp Cys Ser Val Gin Arg Arg His Gin Lys He He Glu Glu Ala Pro 35 40 45 Ala Ala He Ala Thr Pro Ala Val Phe Glu His Met Glu Gin Cys Ala 50 55 60 Val Lys Leu Ala Lys Met Val Gly Tyr Val Ser Ala Gly Thr Val Glu 65 70 75 80 Tyr Leu Tyr Ser Gin Asp 85 (2) INFORMATION FOR SEQ ID NO:11: (i) Sequence characteristics: (A) Length: 70 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:11: Gly Ser Phe Tyr Phe Leu Glu Leu Asn Pro Arg Leu Gin Val Glu His 5 10 15 Pro Cys Thr Glu Met Val Ala Asp Val Asn Leu Pro Ala Ala Gin Leu 20 25 30 Gin He Ala Met Gly He Pro Leu Phe Arg He Lys Asp He Arg Met 35 40 45 Met Tyr Gly Val Ser Pro Trp Gly Asp Ala Pro He Asp Phe Glu Asn 50 55 60 Ser Ala His Val Pro Cys 65 70 (2) INFORMATION FOR SEQ ID NO:12: (i) Sequence characteristics: (A) Length: 20 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:12: Pro Arg Gly His Val He Ala Ala Arg He Thr Ser Glu Asn Pro Asp 5 10 15 Glu Gly Phe Lys 20 (2) INFORMATION FOR SEQ ID NO:13: (i) Sequence characteristics: (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:13: Pro Ser Ser Gly Thr Val Gin Glu Leu Asn Phe Arg Ser Asn Lys Asn 5 10 15 Val Trp Gly Tyr Phe 20 (2) INFORMATION FOR SEQ ID NO:14: (i) Sequence characteristics: (A) Length: 122 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:14: Ser Val Ala Ala Ala Gly Gly Leu His Glu Phe Ala Asp Ser Gin Phe 5 10 15 Gly His Cys Phe Ser Trp Gly Glu Asn Arg Glu Glu Ala He Ser Asn 20 25 30 Met Val Val Ala Leu Lys Glu Leu Ser He Arg Gly Asp Phe Arg Thr 35 40 45 Thr Val Glu Tyr Leu He Lys Leu Leu Glu Thr Glu Ser Phe Gin Leu 50 55 60 Asn Arg He Asp Thr Gly Trp Leu Asp Arg Leu He Ala Glu Lys Val 65 70 75 80 Gin Ala Glu Arg Pro Asp Thr Met Leu Gly Val Val Cys Gly Ala Leu 85 90 95 His Val Ala Asp Val Asn Leu Arg Asn Ser He Ser Asn Phe Leu His 100 105 110 Ser Leu Glu Arg Gly Gin Val Leu Pro Ala 115 120 (2) INFORMATION FOR SEQ ID NO:15: (i) Sequence characteristics: (A) Length: 190 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:15: His Thr Leu Leu Asn Thr Val Asp Val Glu Leu He Tyr Glu Gly He 5 10 15 Lys Tyr Val Leu Lys Val Thr Arg Gin Ser Pro Asn Ser Tyr Val Val 20 25 30 He Met Asn Gly Ser Cys Val Glu Val Asp Val His Arg Leu Ser Asp 35 40 45 Gly Gly Leu Leu Leu Ser Tyr Asp Gly Ser Ser Tyr Thr Thr Tyr Met 50 55 60 Lys Glu Glu Val Asp Arg Tyr Arg He Thr He Gly Asn Lys Thr Cys 65 70 75 80 Val Phe Glu Lys Glu Asn Asp Pro Ser Val Met Arg Ser Pro Ser Ala 85 90 95 Gly Lys Leu He Gin Tyr He Val Glu Asp Gly Gly His Val Phe Ala 100 105 110 Gly Gin Cys Tyr Ala Glu He Glu Val Met Lys Met Val Met Thr Leu 115 120 125 Thr Ala Val Glu Ser Gly Cys He His Tyr Val Lys Arg Pro Gly Ala 130 135 140 Ala Leu Asp Pro Gly Cys Val He Ala Lys Met Gin Leu Asp Asn Pro 145 150 155 160 Ser Lys Val Gin Gin Ala Glu Leu His Thr Gly Ser Leu Pro Gin He 165 170 175 Gin Ser Thr Ala Leu Arg Gly Glu Lys Leu His Arg He Phe 180 185 190 (2) INFORMATION FOR SEQ ID NO:16: (i) Sequence characteristics: (A) Length: 37 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:16: Val Met He Lys Ala Ser Trp Gly Gly Gly Gly Lys Gly He Arg Lys 5 10 15 Val His Asn Asp Asp Glu Val Arg Ala Leu Phe Lys Gin Val Gin Gly 20 25 30 Glu Val Pro Gly Ser 35 (2) INFORMATION FOR SEQ ID NO:17: (i) Sequence characteristics: (A) Length: 187 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:17: Pro He Phe He Met Lys Val Ala Ser Gin Ser Arg His Leu Glu Val 5 10 15 Gin Leu Leu Cys Asp Lys His Gly Asn Val Ala Ala Leu His Ser Arg 20 25 30 Asp Cys Ser Val Gin Arg Arg His Gin Lys He He Glu Glu Gly Pro 35 40 45 He Thr Val Ala Pro Pro Glu Thr He Lys Glu Leu Glu Gin Ala Ala 50 55 60 Arg Arg Leu Ala Lys Cys Val Gin Tyr Gin Gly Ala Ala Thr Val Glu 65 70 75 80 Tyr Leu Tyr Ser Met Glu Thr Gly Glu Tyr Tyr Phe Leu Glu Leu Asn 85 90 95 Pro Arg Leu Gin Val Glu His Pro Val Thr Glu Trp He Ala Glu He 100 105 110 Asn Leu Pro Ala Ser Gin Val Val Val Gly Met Gly He Pro Leu Tyr 115 120 125 Asn He Pro Glu He Arg Arg Phe Tyr Gly He Glu His Gly Gly Gly 130 135 140 Tyr His Ala Trp Lys Glu He Ser Ala Val Ala Thr Lys Phe Asp Leu 145 150 155 160 Asp Lys Ala Gin Ser Val Lys Pro Lys Gly His Cys Val Ala Val Arg 165 170 175 Val Thr Ser Glu Asp Pro Asp Asp Gly Phe Lys 180 185 (2) INFORMATION FOR SEQ ID NO:18: (i) Sequence characteristics: (A) Length: 21 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:18: Pro Thr Ser Gly Arg Val Glu Glu Leu Asn Phe Lys Ser Lys Pro Asn 5 10 15 Val Trp Ala Tyr Phe 20 (2) INFORMATION FOR SEQ ID NO:19: (i) Sequence characteristics: (A) Length: 122 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:19: Ser Val Lys Ser Gly Gly Ala He His Glu Phe Ser Asp Ser Gin Phe 5 10 15 Gly His Val Phe Ala Phe Gly Glu Ser Arg Ser Leu Ala He Ala Asn 20 25 30 Met Val Leu Gly Leu Lys Glu He Gin He Arg Gly Glu He Arg Thr 35 40 45 Asn Val Asp Tyr Thr Val Asp Leu Leu Asn Ala Ala Glu Tyr Arg Glu 50 55 60 Asn Met He His Thr Gly Trp Leu Asp Ser Arg He Ala Met Arg Val 65 70 75 80 Arg Ala Glu Arg Pro Pro Trp Tyr Leu Ser Val Val Gly Gly Ala Leu 85 90 95 Tyr Glu Ala Ser Ser Arg Ser Ser Ser Val Val Thr Asp Tyr Val Gly 100 105 110 Tyr Leu Ser Lys Gly Gin He Pro Pro Lys 110 120 (2) INFORMATION FOR SEQ ID NO:20: (i) Sequence characteristics: (A) Length: 124 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:20: His He Ser Leu Val Asn Leu Thr Val Thr Leu Asn He Asp Gly Ser 5 10 15 Lys Tyr Thr He Glu Thr Val Arg Gly Gly Pro Arg Ser Tyr Lys Leu 20 25 30 Arg He Asn Glu Ser Glu Val Glu Ala Glu He His Phe Leu Arg Asp 35 40 45 Gly Gly Leu Leu Met Gin Leu Asp Gly Asn Ser His Val He Tyr Ala 50 55 60 Glu Thr Glu Ala Ala Gly Thr Arg Leu Leu He Asn Gly Arg Thr Cys 65 70 75 80 Leu Leu Gin Lys Glu His Asp Pro Ser Arg Leu Leu Ala Asp Thr Pro 85 90 95 Cys Lys Leu Leu Arg Phe Leu Val Ala Asp Gly Ser His Val Val Ala 100 105 110 Asp Thr Pro Tyr Ala Glu Val Glu Ala Met Lys Met 115 120 (2) INFORMATION FOR SEQ ID NO:21: (i) Sequence characteristics: (A) Length: 222 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:21: Met Glu Glu Ser Ser Gin Pro Ala Lys Pro Leu Glu Met Asn Pro His 5 10 15 Ser Arg Phe He He Gly Ser Val Ser Glu Asp Asn Ser Glu Asp Glu 20 25 30 Thr Ser Ser Leu Val Lys Leu Asp Leu Leu Glu Glu Lys Glu Arg Ser 35 40 45 Leu Ser Pro Val Ser Val Cys Ser Asp Ser Leu Ser Asp Leu Gly Leu 50 55 60 Pro Ser Ala Gin Asp Gly Leu Ala Asn His Met Arg Pro Ser Met Ser 65 70 75 80 Gly Leu His Leu Val Lys Gin Gly Arg Asp Arg Lys Lys Val Asp Val 85 90 95 Gin Arg Asp Phe Thr Val Ala Ser Pro Ala Glu Phe Val Thr Arg Phe 100 105 110 Gly Gly Asn Arg Val He Glu Lys Val Leu He Ala Asn Asn Gly He 115 120 125 Ala Ala Val Lys Cys Met Arg Ser He Arg Arg Trp Ser Tyr Glu Met 130 135 140 Phe Arg Asn Glu Arg Ala He Arg Phe Val Val Met Val Thr Pro Glu 145 150 155 160 Asp Leu Lys Ala Asn Ala Glu Tyr He Lys Met Ala Asp His Tyr Val 165 170 175 Pro Val Pro Gly Gly Pro Asn Asn Asn Asn Tyr Ala Asn Val Glu Leu 180 185 190 He Leu Asp He Ala Lys Arg He Pro Val Gin Ala Val Trp Ala Gly 195 200 205 Trp Gly His Ala Ser Glu Asn Pro Lys Leu Pro Glu Leu Leu 210 215 220 (2) INFORMATION FOR SEQ ID NO:22: (i) Sequence characteristics: (A) Length: 122 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:22: His Lys Asn Gly He Ala Phe Met Gly Pro Pro Ser Gin Ala Met Trp 5 10 15 Ala Leu Gly Asp Lys He Ala Ser Ser He Val Ala Gin Thr Ala Gly 20 25 30 He Pro Thr Leu Pro Trp Asn Gly Ser Gly Leu Arg Val Asp Trp Gin 35 40 45 Glu Asn Asp Leu Gin Lys Arg He Leu Asn Val Pro Gin Glu Leu Tyr 50 55 60 Glu Lys Gly Tyr Val Lys Asp Ala Asp Asp Gly Leu Arg Ala Ala Glu 65 70 75 80 Glu Val Gly Tyr Pro Val Met He Lys Ala Ser Glu Gly Gly Gly Gly 85 90 95 Lys Gly He Arg Lys Val Asn Asn Ala Asp Asp Phe Pro Asn Leu Phe 100 105 110 Arg Gin Val Gin Ala Glu Val Pro Gly Ser 115 120 (2) INFORMATION FOR SEQ ID NO:23: (i) Sequence characteristics: (A) Length: 95 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:23: Pro He Phe Val Met Arg Leu Ala Lys Gin Ser Arg His Leu Glu Val 5 10 15 Gin He Leu Ala Asp Gin Tyr Gly Asn Ala He Ser Leu Phe Gly Arg 20 25 30 Asp Cys Ser Val Gin Arg Arg His Gin Lys He He Glu Glu Ala Gly 35 40 45 Leu Arg Ala Ala Glu Glu Val Gly Tyr Pro Val Met He Lys Ala Ser 50 55 60 Glu Gly Gly Gly Gly Lys Gly He Arg Lys Val Asn Asn Ala Asp Asp 65 70 75 80 Phe Pro Asn Leu Phe Arg Gin Val Gin Ala Glu Val Pro Gly Ser 80 90 95 (2) INFORMATION FOR SEQ ID NO:24: (i) Sequence characteristics: (A) Length: 86 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:24: Pro He Phe Val Met Arg Leu Ala Lys Gin Ser Arg His Leu Glu Val 5 10 15 Gin He Leu Ala Asp Gin Tyr Gly Asn Ala He Ser Leu Phe Gly Arg 20 25 30 Asp Cys Ser Val Gin Arg Arg His Gin Lys He He Glu Glu Ala Pro 35 40 45 Ala Ser He Ala Thr Ser Val Val Phe Glu His Met Glu Gin Cys Ala 50 55 60 Val Lys Leu Ala Lys Met Val Gly Tyr Val Ser Ala Gly Thr Val Glu 65 70 75 80 Tyr Leu Tyr Ser Gin Asp 85 (2) INFORMATION FOR SEQ ID NO:25: (i) Sequence characteristics: (A) Length: 70 amino acids (B) Type: Amino acids (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:25: Gly Ser Phe Tyr Phe Leu Glu Leu Asn Pro Arg Leu Gin Val Glu His 5 10 15 Pro Cys Thr Glu Met Val Ala Asp Val Asn Leu Pro Ala Ala Gin Leu 20 25 30 Gin He Ala Met Gly He Pro Leu His Arg He Lys Asp He Arg Val 35 40 45 Met Tyr Gly Val Ser Pro Trp Gly Asp Gly Ser He Asp Phe Glu Asn 50 35 60 Ser Ala His Val Pro Cys 65 70 (2) INFORMATION FOR SEQ ID NO:26: (i) Sequence characteristics: (A) Length: 20 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:26: Pro Arg Gly His Val He Ala Ala Arg He Thr Ser Glu Asn Pro Asp 5 10 15 Glu Gly Phe Lys 20 (2) INFORMATION FOR SEQ ID NO:27: (i) Sequence characteristics: (A) Length: 21 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:27: Pro Ser Ser Gly Thr Val Gin Glu Leu Asn Phe Arg Ser Asn Lys Asn 5 10 15 Val Trp Gly Tyr Phe 20 (2) INFORMATION FOR SEQ ID NO:28: (i) Sequence characteristics: (A) Length: 122 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:28: Ser Val Ala Ala Ala Gly Gly Leu His Glu Phe Ala Asp Ser Gin Phe 5 10 15 Gly His Cys Phe Ser Trp Gly Glu Asn Arg Glu Glu Ala He Ser Asn 20 25 30 Met Val Val Ala Leu Lys Glu Leu Ser He Arg Gly Asp Phe Arg Thr 35 40 45 Thr Val Glu Tyr Leu He Lys Leu Leu Glu Thr Glu Ser Phe Gin Gin 50 55 60 Asn Arg He Asp Thr Gly Trp Leu Asp Arg Leu He Ala Glu Lys Val 65 70 75 80 Gin Ala Glu Arg Pro Asp Thr Met Leu Gly Val Val Cys Gly Ala Leu 85 90 95 His Val Ala Asp Val Ser Phe Arg Asn Ser Val Ser Asn Phe Leu His 100 105 110 Ser Leu Glu Arg Gly Gin Val Leu Pro Ala 115 120 (2) INFORMATION FOR SEQ ID NO:29: (i) Sequence characteristics: (A) Length: 90 amino acids (B) Type: Amino acid (C) strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID N0:29: Met Val Val Ala Leu Lys Glu Leu Ser He Arg Gly Asp Phe Arg Thr 5 10 15 Thr Val Glu Tyr Leu He Lys Leu Leu Glu Thr Glu Ser Phe Gin Gin 20 25 30 Asn Arg He Asp Thr Gly Trp Leu Asp Arg Leu He Ala Glu Lys Val 35 40 45 Gin Ala Glu Arg Pro Asp Thr Met Leu Gly Val Val Cys Gly Ala Leu 50 55 60 His Val Ala Asp Val Ser Phe Arg Asn Ser Val Ser Asn Phe Leu His 65 70 75 80 Ser Leu Glu Arg Gly Gin Val Leu Pro Ala 85 90 (2) INFORMATION FOR SEQ ID NO:30: (i) Sequence characteristics: (A) Length: 190 amino acids (B) Type: Amino acid (C) strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:30: His Thr Leu Leu Asn Thr Val Asp Val Glu Leu He Tyr Glu Gly Arg 5 10 15 Lys Tyr Val Leu Lys Val Thr Arg Gin Ser Pro Asn Ser Tyr Val Val 20 25 30 He Met Asn Ser Ser Cys Val Glu Val Asp Val His Arg Leu Ser Asp 35 40 45 Gly Gly Leu Leu Leu Ser Tyr Asp Gly Ser Ser Tyr Thr Thr Tyr Met 50 55 60 Lys Glu Glu Val Asp Arg Tyr Arg He Thr He Gly Asn Lys Thr Cys 65 70 75 80 Val Phe Glu Lys Glu Asn Asp Pro Ser He Leu Arg Ser Pro Ser Ala 85 90 95 Gly Lys Leu He Gin Tyr Val Val Glu Asp Gly Gly His Val Phe Ala 100 105 110 Gly Gin Cys Phe Ala Glu He Glu Val Met Lys Met Val Met Thr Leu 115 120 125 Thr Ala Gly Glu Ser Gly Cys He His Tyr Val Lys Arg Pro Gly Ala 130 135 140 Val Leu Asp Pro Gly Cys Val He Ala Lys Leu Gin Leu Asp Asp Pro 145 150 155 160 Ser Arg Val Gin Gin Ala Glu Leu His Thr Gly Thr Leu Pro Gin He 165 170 175 Gin Ser Thr Ala Leu Arg Gly Glu Lys Leu His Arg He Phe 180 185 190 (2) INFORMATION FOR SEQ ID NO:31: (i) Sequence characteristics: (A) Length: 41 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:31: Met Ser Glu Glu Ser Leu Phe Glu Ser Ser Pro Gin Lys Met Glu Tyr 5 10 15 Glu He Thr Asn Tyr Ser Glu Arg His Thr Glu Leu Pro Gly His Phe 20 25 30 He Gly Leu Asn Thr Val Asp Lys Leu 35 40 (2) INFORMATION FOR SEQ ID NO:32: (i) Sequence characteristics: (A) Length: 74 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:32: Ala Asp Val Asp Ala Val Trp Ala Gly Trp Gly His Ala Ser Glu Asn 5 10 15 Pro Leu Leu Pro Glu Lys Leu Ser Gin Ser Lys Arg Lys Val He Phe 20 25 30 He Gly Pro Pro Gly Asn Ala Met Arg Ser Leu Gly Asp Lys He Ser 35 40 45 Ser Thr Thr He Val Ala Gin Ser Ala Lys Val Pro Cys He Pro Trp 50 55 60 Ser Gly Thr Thr Gly Val Asp Thr Val His 65 70 (2) INFORMATION FOR SEQ ID NO:33: (i) Sequence characteristics: (A) Length: 73 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:33: Val Asp Glu Lys Thr Gly Leu Val Ser Val Asp Asp Asp He Tyr Gin 5 10 15 Lys Gly Cys Cys Thr Ser Pro Glu Asp Gly Leu Gin Lys Ala Lys Arg 20 25 30 He Gly Phe Pro Val Met He Lys Ala Ser Glu Gly Gly Gly Gly Lys 35 40 45 Gly He Arg Gin Val Glu Arg Glu Glu Asp Phe He Ala Leu Tyr His 50 55 60 Gin Ala Ala Asn Glu He Pro Gly Ser 65 70 (2) INFORMATION FOR SEQ ID NO:34: (i) Sequence characteristics: (A) Length: 157 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:34: Pro He Phe He Met Lys Leu Ala Gly Arg Ala Arg His Leu Glu Val 5 10 15 Gin Leu Leu Ala Asp Gin Tyr Gly Thr Asn He Ser Leu Phe Gly Arg 20 25 30 Asp Cys Ser Val Gin Arg Arg His Gin Lys He He Glu Glu Ala Pro 35 40 45 Val Thr He Ala Lys Ala Glu Thr Phe His Glu Met Glu Lys Ala Ala 50 55 60 Val Arg Leu Gly Lys Leu Val Gly Tyr Val Ser Ala Gly Thr Val Glu 65 70 75 80 Tyr Leu Tyr Ser His Asp Asp Gly Lys Phe Tyr Phe Leu Glu Leu Asn 85 90 95 Pro Arg Leu Gin Val Glu His Pro Thr Thr Glu Met Val Ser Gly Val 100 105 110 Asn Leu Pro Ala Ala Gin Leu Gin He Ala Met Gly He Pro Met His 115 120 125 Arg He Ser Asp He Arg Thr Leu Tyr Gly Met Asn Pro His Ser Ala 130 135 140 Ser Glu He Asp Phe Glu Phe Lys Thr Gin Asp Ala Thr 145 150 155 (2) INFORMATION FOR SEQ ID NO:35: (i) Sequence characteristics: (A) Length: 27 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:35: Lys Lys Gin Arg Arg Pro He Pro Lys Gly His Cys Thr Ala Cys Arg 5 10 15 He Thr Ser Glu Asp Pro Asn Asp Gly Phe Lys 20 25 (2) INFORMATION FOR SEQ ID NO:36: (i) Sequence characteristics: (A) Length: 21 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:36: Pro Ser Gly Gly Thr Leu His Glu Leu Asn Phe Arg Ser Ser Ser Asn 5 10 15 Val Trp Gly Tyr Phe 20 (2) INFORMATION FOR SEQ ID NO:37: (i) Sequence characteristics: (A) Length: 122 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:37: Ser Val Gly Asn Asn Gly Asn He His Ser Phe Ser Asp Ser Gin Phe 5 10 Gly His He Phe Ala Phe Gly Glu Asn Arg Gin Ala Ser Arg Lys His 20 25 30 Met Val Val Ala Leu Lys Glu Leu Ser He Arg Gly Asp Phe Arg Thr 35 40 45 Thr Val Glu Tyr Leu He Lys Leu Leu Glu Thr Glu Asp Phe Glu Asp 50 55 60 Asn Thr He Thr Thr Gly Trp Leu Asp Asp Leu He Thr His Lys Met 65 70 75 80 Thr Ala Glu Lys Pro Asp Pro Thr Leu Ala Val He Cys Gly Ala Ala 85 90 95 Thr Lys Ala Phe Leu Ala Ser Glu Glu Ala Arg His Lys Tyr He Glu 100 105 110 Ser Leu Gin Lys Gly Gin Val Leu Ser Lys 115 120 (2) INFORMATION FOR SEQ ID NO:38: (i) Sequence characteristics: (A) Length: 190 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:38: Asp Leu Leu Gin Thr Met Phe Pro Val Asp Phe He His Glu Gly Lys 5 10 15 Arg Tyr Lys Phe Thr Val Ala Lys Ser Gly Asn Asp Arg Tyr Thr Leu 20 25 30 Phe He Asn Gly Ser Lys Cys Asp He He Leu Arg Gin Leu Ser Asp 35 40 45 Gly Gly Leu Leu He Ala He Gly Gly Lys Ser His Thr He Tyr Trp 50 55 60 Lys Glu Glu Val Ala Ala Thr Arg Leu Ser Val Asp Ser Met Thr Thr 65 70 75 80 Leu Leu Glu Val Glu Asn Asp Pro Thr Gin Leu Arg Thr Pro Ser Pro 85 90 95 Gly Lys Leu Val Lys Phe Leu Val Glu Asn Gly Glu His He He Lys 100 105 110 Gly Gin Pro Tyr Ala Glu He Glu Val Met Lys Met Gin Met Pro Leu 115 120 125 Val Ser Gin Glu Asn Gly He Val Gin Leu Leu Lys Gin Pro Gly Ser 130 135 140 Thr He Val Ala Gly Asp He Met Ala He Met Thr Leu Asp Asp Pro 145 150 155 160 Ser Lys Val Lys His Ala Leu Pro Phe Glu Gly Met Leu Pro Asp Phe 165 170 175 Gly Ser Pro Val He Glu Gly Thr Lys Pro Ala Tyr Lys Phe 180 185 190 (2) INFORMATION FOR SEQ ID NO:39: (i) Sequence characteristics: (A) Length: 37 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:39: Met Arg Phe Asn Lys He Leu He Ala Asn Arg Gly Glu He Ala Leu 5 10 15 Arg He Leu Arg Thr Cys Glu Glu Leu Gly He Gly Thr He Ala Val 20 25 30 His Ser Thr Val Asp 35 (2) INFORMATION FOR SEQ ID NO: 0: (i) Sequence characteristics: (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:40: Arg Asn Ala Leu His Val Gin Leu Ala Asp Glu Ala Val Cys He Gly 5 10 15 Glu Ala Ala Ser Ser 20 (2) INFORMATION FOR SEQ ID NO: 1: (i) Sequence characteristics: (A) Length: 38 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:41: Lys Ser Tyr Leu Asn He Pro Asn He He Ala Ala Ala Leu Thr Arg 5 10 15 Asn Ala Ser Ala He His Pro Gly Tyr Gly Phe Leu Ala Glu Asn Ala 20 25 30 Arg Phe Ala Glu He Cys 35 (2) INFORMATION FOR SEQ ID NO: 2: (i) Sequence characteristics: (A) Length: 41 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:42: Ala Asp His His Leu Thr Phe He Gly Pro Ser Pro Asp Ser He Arg 5 10 15 Ala Met Gly Asp Lys Ser Thr Ala Lys Glu Thr Met Gin Arg Val Gly 20 25 30 Val Pro Thr He Pro Gly Ser Asp Gly 35 40 (2) INFORMATION FOR SEQ ID NO: 3: (i) Sequence characteristics: (A) Length: 143 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:43: Leu Leu Thr Asp Val Asp Ser Ala Ala Lys Val Ala Ala Glu He Gly 5 10 15 Tyr Pro Val Met He Lys Ala Thr Ala Gly Gly Gly Gly Arg Gly Met 20 25 30 Arg Leu Val Arg Glu Pro Ala Asp Leu Glu Lys Leu Phe Leu Ala Ala 35 40 45 Gin Gly Glu Ala Glu Ala Ala Phe Gly Asn Pro Gly Leu Tyr Leu Glu 50 55 60 Lys Phe He Asp Arg Pro Arg His Val Glu Phe Gin He Leu Ala Asp 65 70 75 80 Ala Tyr Gly Asn Val Val His Leu Gly Glu Arg Asp Cys Ser He Gin 85 90 95 Arg Arg His Gin Lys Leu Leu Glu Glu Ala Pro Ser Pro Ala Leu Ser 100 105 110 Ala Asp Leu Arg Gin Lys Met Gly Asp Ala Ala Val Lys Val Ala Gin 115 120 125 Ala He Gly Tyr He Gly Ala Gly Thr Val Glu Phe Leu Val Asp 130 135 140 (2) INFORMATION FOR SEQ ID NO: 4: (i) Sequence characteristics: (A) Length: 50 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:44: Ala Thr Gly Asn Phe Tyr Phe Met Glu Met Asn Thr Arg He Gin Val 5 10 15 Glu His Pro Val Thr Glu Met He Thr Gly Leu Asp Leu He Ala Glu 20 25 30 Gin He Arg He Ala Gin Gly Glu Ala Leu Arg Phe Arg Gin Ala Asp 35 40 45 He Gin 50 (2) INFORMATION FOR SEQ ID NO: 5: (i) Sequence characteristics: (A) Length: 19 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:45: Leu Arg Gly His Ala He Glu Cys Arg He Asn Ala Glu Asp Pro Glu 5 10 15 Tyr Asn Phe (2) INFORMATION FOR SEQ ID NO:46: (i) Sequence characteristics: (A) Length: 9 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:46: Arg Pro Asn Pro Gly Arg He Thr Gly 5 (2) INFORMATION FOR SEQ ID NO: 7: (i) Sequence characteristics: (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:47: Pro Gly Val Arg Val Asp Ser 5 (2) INFORMATION FOR SEQ ID NO:48: (i) Sequence characteristics: (A) Length: 44 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:48: His Val Tyr Thr Asp Tyr Glu He Pro Pro Tyr Tyr Asp Ser Leu He 5 10 15 Gly Lys Leu He Val Trp Gly Ala Thr Arg Glu Glu Ala He Ala Arg 20 25 30 Met Gin Arg Ala Leu Arg Glu Cys Ala He Thr Gly 35 40 (2) INFORMATION FOR SEQ ID NO:49: (i) Sequence characteristics: (A) Length: 38 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:49: Leu Pro Thr Thr Leu Ser Phe His Gin Leu Met Leu Gin Met Pro Glu 5 10 15 Phe Leu Arg Gly Glu Leu Tyr Thr Asn Phe Val Glu Gin Val Met Leu 20 25 30 Pro Arg He Leu Lys Ser 35 (2) INFORMATION FOR SEQ ID NO:50: (i) Sequence characteristics: (A) Length: 37 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:50: Met Lys Phe Asp Lys He Leu He Ala Asn Arg Gly Glu He Ala Leu 5 10 15 Arg He Leu Arg Ala Cys Glu Glu Met Gly He Ala Thr He Ala Val 20 25 30 His Ser Thr Val Asp 35 (2) INFORMATION FOR SEQ ID NO:51: (i) Sequence characteristics: (A) Length: 21 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:51: Arg Asn Ala Leu His Val Gin Leu Ala Asp Glu Ala Val Cys He Gly 5 10 15 Glu Pro Ala Ser Ala 20 (2) INFORMATION FOR SEQ ID NO:52: (i) Sequence characteristics: (A) Length: 38 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:52: Lys Ser Tyr Leu Asn He Pro Asn He He Ala Ala Ala Leu Thr Arg 5 10 15 Asn Ala Ser Ala He His Pro Gly Tyr Gly Phe Leu Ser Glu Asn Ala 20 25 30 Lys Phe Ala Glu He Cys 35 (2) INFORMATION FOR SEQ ID NO:53: (i) Sequence characteristics: (A) Length: 42 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:53: Ala Asp His His He Ala Phe He Gly Pro Thr Pro Glu Ala He Arg 5 10 15 Leu Met Gly Asp Lys Ser Thr Ala Lys Glu Thr Met Gin Lys Ala Gly 20 25 30 Val Pro Thr Val Pro Gly Ser Glu Gly Leu 35 40 (2) INFORMATION FOR SEQ ID NO:54: (i) Sequence characteristics: (A) Length: 142 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:54: Val Glu Thr Glu Gin Glu Gly Leu Glu Leu Ala Lys Asp He Gly Tyr 5 10 15 Pro Val Met He Lys Ala Thr Ala Gly Gly Gly Gly Arg Gly Met Arg 20 25 30 Leu Val Arg Ser Pro Asp Glu Phe Val Lys Leu Phe Leu Ala Ala Gin 35 40 45 Gly Glu Ala Gly Ala Ala Phe Gly Asn Ala Gly Val Tyr He Glu Lys 50 55 60 Phe He Glu Arg Pro Arg His He Glu Phe Gin He Leu Ala Asp Asn 65 70 75 80 Tyr Gly Asn Val He His Leu Gly Glu Arg Asp Cys Ser He Gin Arg 85 90 95 Arg Asn Gin Lys Leu Leu Glu Glu Ala Pro Ser Pro Ala Leu Asp Ser 100 105 110 Asp Leu Arg Glu Lys Met Gly Gin Ala Ala Val Lys Ala Ala Gin Phe 115 120 125 He Asn Tyr Ala Gly Ala Gly Thr He Glu Phe Leu Leu Asp 130 135 140 (2) INFORMATION FOR SEQ ID NO:55: (i) Sequence characteristics: (A) Length: 50 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:55: Arg Ser Gly Gin Phe Tyr Phe Met Glu Met Asn Thr Arg He Gin Val 5 10 15 Glu His Pro Val Thr Glu Met Val Thr Gly Val Asp Leu Leu Val Glu 20 25 30 Gin He Arg He Ala Gin Gly Glu Arg Leu Arg Leu Thr Gin Asp Gin 35 40 45 Val Val 50 (2) INFORMATION FOR SEQ ID NO:56: (i) Sequence characteristics: (A) Length: 19 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:56: Leu Arg Gly His Ala He Glu Cys Arg He Asn Ala Glu Asp Pro Asp 5 10 15 His Asp Phe (2) INFORMATION FOR SEQ ID NO:57: (i) Sequence characteristics: (A) Length: 9 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:57: Arg Pro Ala Pro Gly Arg He Ser Gly 5 (2) INFORMATION FOR SEQ ID NO:58: (i) Sequence characteristics: (A) Length: 6 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:58: Tyr Leu Pro Pro Gly Gly 5 (2) INFORMATION FOR SEQ ID NO:59: (i) Sequence characteristics: (A) Length: 7 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:59: Pro Gly Val Arg He Asp Ser 5 (2) INFORMATION FOR SEQ ID NO:60: (i) Sequence characteristics: (A) Length: 44 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:60: His Val Tyr Thr Asp Tyr Gin He Pro Pro Tyr Tyr Asp Ser Leu He 5 10 15 Gly Lys Leu He Val Trp Gly Pro Asp Arg Ala Thr Ala He Asn Arg 20 25 30 Met Lys Arg Ala Leu Arg Glu Cys Ala He Thr Gly 35 40 (2) INFORMATION FOR SEQ ID NO:61: (i) Sequence characteristics: (A) Length: 154 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: inear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:61: Leu Pro Thr Thr He Gly Phe His Gin Arg He Met Glu Asn Pro Gin 5 10 15 Phe Leu Gin Gly Asn Val Ser Thr Ser Phe Val Gin Glu Met Asn Lys 20 25 30 Pro Leu Asp Phe Asn Glu He Arg Gin Leu Leu Thr Thr He Ala Gin 35 40 45 Thr Asp He Ala Glu Val Thr Leu Lys Ser Asp Asp Phe Glu Leu Thr 50 55 60 Val Arg Lys Ala Val Gly Val Asn Asn Ser Val Val Pro Val Val Thr 65 50 75 80 Ala Pro Leu Ser Gly Val Val Gly Ser Gly Leu Pro Ser Ala He Pro 85 90 95 He Val Ala His Ala Ala Pro Ser Pro Ser Pro Glu Pro Gly Thr Ser 100 105 110 Arg Ala Ala Asp His Ala Val Thr Ser Ser Gly Ser Gin Pro Gly Ala 115 120 125 Lys He He Asp Gin Lys Leu Ala Glu Val Ala Ser Pro Met Val Gly 130 135 140 Thr Phe Tyr Arg Ala Pro Ala Pro Gly Glu 145 150 (2) INFORMATION FOR SEQ ID NO:62: (i) Sequence characteristics: (A) Length: 24 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:62: Ala Val Phe Val Glu Val Gly Asp Arg He Arg Gin Gly Gin Thr Val 5 10 15 Cys He He Glu Ala Met Lys Met 20 (2) INFORMATION FOR SEQ ID NO:63: (i) Sequence characteristics: (A) Length: 36 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:63: Met Leu Asp Lys He Val He Ala Asn Arg Gly Glu He Ala Leu Arg 5 10 15 He Leu Arg Ala Cys Lys Glu Leu Gly He Lys Thr Val Ala Val His 20 25 30 Ser Ser Ala Asp 35 (2) INFORMATION FOR SEQ ID NO: 4: (i) Sequence characteristics: (A) Length: 21 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:64: Arg Asp Leu Lys His Val Leu Leu Ala Asp Glu Thr Val Cys He Gly 5 10 15 Pro Ala Pro Ser Val 20 (2) INFORMATION FOR SEQ ID NO:65: (i) Sequence characteristics: (A) Length: 38 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:65: Lys Ser Tyr Leu Asn He Pro Ala He He Ser Ala Ala Glu He Thr 5 10 15 Gly Ala Val Ala He His Pro Gly Tyr Gly Phe Leu Ser Glu Asn Ala 20 25 30 Asn Phe Ala Glu Gin Val 35 (2) INFORMATION FOR SEQ ID NO:66: (i) Sequence characteristics: (A) Length: 43 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:66: Glu Arg Ser Gly Phe He Phe He Gly Pro Lys Ala Glu Thr He Arg 5 10 15 Leu Met Gly Asp Lys Val Ser Ala He Ala Ala Met Lys Lys Ala Gly 20 25 30 Val Pro Cys Val Pro Gly Ser Asp Gly Pro Leu 35 40 (2) INFORMATION FOR SEQ ID NO:67: (i) Sequence characteristics: (A) Length: 141 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:67: Gly Asp Asp Met Asp Lys Asn Arg Ala He Ala Lys Arg He Gly Tyr 5 10 15 Pro Val He He Lys Ala Ser Gly Gly Gly Gly Gly Arg Gly Met Arg 20 25 30 Val Val Arg Gly Asp Ala Glu Leu Ala Gin Ser He Ser Met Thr Arg 35 40 45 Ala Glu Ala Lys Ala Ala Phe Ser Asn Asp Met Val Tyr Met Glu Lys 50 55 60 Tyr Leu Glu Asn Pro Arg His Val Glu He Gin Val Leu Ala Asp Gly 65 70 75 80 Gin Gly Asn Ala He Tyr Leu Ala Glu Arg Asp Cys Ser Met Gin Arg 85 90 95 Arg His Gin Lys Val Val Glu Glu Ala Pro Ala Pro Gly He Thr Pro 100 105 110 Glu Leu Arg Arg Tyr He Gly Glu Arg Cys Ala Lys Ala Cys Val Asp 115 120 125 He Gly Tyr Arg Gly Ala Gly Thr Phe Glu Phe Leu Phe 130 135 140 (2) INFORMATION FOR SEQ ID NO:68: (i) Sequence characteristics: (A) Length: 50 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:68: Glu Asn Gly Glu Phe Tyr Phe He Glu Met Asn Thr Arg He Gin Val 5 10 15 Glu His Pro Val Thr Glu Met He Thr Gly Val Asp Leu He Lys Glu 20 25 30 Gin Met Arg He Ala Ala Gly Gin Pro Leu Ser He Lys Gin Glu Glu 35 40 45 Val His 50 (2) INFORMATION FOR SEQ ID NO:69: (i) Sequence characteristics: (A) Length: 25 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:69: Val Arg Gly His Ala Val Glu Cys Arg He Asn Ala Glu Asp Pro Asn 5 10 15 Leu Pro Ser Pro Gly Lys He Thr Arg 20 25 (2) INFORMATION FOR SEQ ID NO:70: (i) Sequence characteristics: (A) Length: 6 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:70: Phe His Ala Pro Gly Gly 5 (2) INFORMATION FOR SEQ ID NO:71: (i) Sequence characteristics: (2) INFORMATION FOR SEQ ID NO:72: (i) Sequence characteristics: (A) Length: 44 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:72: His He Tyr Ala Gly Tyr Thr Val Pro Pro Tyr Tyr Asp Ser Met He 5 10 15 Gly Lys Leu He Cys Tyr Gly Glu Asn Arg Asp Val Ala He Ala Arg 20 25 30 Met Lys Asn Ala Leu Gin Glu Leu He He Asp Gly 35 40 (2) INFORMATION FOR SEQ ID NO:73: (i) Sequence characteristics: (A) Length: 135 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:73: He Lys Thr Asn Val Asp Leu Gin He Arg He Met Asn Asp Glu Asn 5 10 15 Phe Gin His Gly Gly Thr Asn He His Tyr Leu Glu Lys Lys Leu Gly 20 25 30 Leu Gin Glu Lys Met Asp He Arg Lys He Lys Lys Leu He Glu Leu 35 40 45 Val Glu Glu Ser Gly He Ser Glu Leu Glu He Ser Glu Gly Glu Glu 50 55 60 Ser Val Arg He Ser Arg Ala Ala Pro Ala Ala Ser Phe Pro Val Met 65 70 75 80 Gin Gin Ala Tyr Ala Ala Pro Met Met Gin Gin Pro Ala Gin Ser Asn 85 90 95 Ala Ala Ala Pro Ala Thr Val Pro Ser Met Glu Ala Pro Ala Ala Ala 100 105 110 Glu He Ser Gly His He Val Arg Ser Pro Met Val Gly Thr Phe Tyr 115 120 125 Arg Thr Pro Ser Pro Asp Ala 130 135 (2) INFORMATION FOR SEQ ID NO:74: (i) Sequence characteristics: (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:74: Lys Ala Phe He Glu Val Gly Gin Lys Val Asn Val Gly Asp Thr Leu 5 10 15 Cys He Val Glu Ala Met Lys Met Met Asn Gin He Glu Ala Asp Lys 20 25 30 Ser Gly Thr Val Lys Ala He Leu Val Glu Ser Gly Gin Pro Val Glu 35 40 45 Phe Asp Glu Pro Leu Val Val He Glu 50 55 (2) INFORMATION FOR SEQ ID NO:75: (i) Sequence characteristics: (A) Length: 72 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:75: Met Leu Ser Ala Ala Leu Arg Thr Leu Lys His Val Leu Tyr Tyr Ser 5 10 15 Arg Gin Cys Leu Met Val Ser Arg Asn Leu Gly Ser Val Gly Tyr Asp 20 25 30 Pro Asn Glu Lys Thr Phe Asp Lys He Leu Val Ala Asn Arg Gly Glu 35 40 45 He Ala Cys Arg Val He Arg Thr Cys Lys Lys Met Gly He Lys Thr 50 55 60 Val Ala He His Ser Asp Val Asp 65 70 (2) INFORMATION FOR SEQ ID NO:76: (i) Sequence characteristics: (A) Length: 21 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:76: Ala Ser Ser Val His Val Lys Met Ala Asp Glu Ala Val Cys Val Gly 5 10 15 Pro Ala Pro Thr Ser 20 (2) INFORMATION FOR SEQ ID NO:77: (i) Sequence characteristics: (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:77: Lys Ser Tyr Leu Asn Met Asp Ala He Met Glu Ala He Lys Lys Thr 5 10 15 Arg Ala Gin Ala Val His Pro Gly Tyr Gly Phe Leu Ser Glu Asn Lys 20 25 30 Glu Phe Ala Arg Cys Leu 35 (2) INFORMATION FOR SEQ ID NO:78: (i) Sequence characteristics: (A) Length: 41 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:78: Ala Ala Glu Asp Val Val Phe He Gly Pro Asp Thr His Ala He Gin 5 10 15 Ala Met Gly Asp Lys He Glu Ser Lys Leu Leu Ala Lys Lys Ala Glu 20 25 30 Val Asn Thr He Pro Gly Phe Asp Gly 35 40 (2) INFORMATION FOR SEQ ID NO:79: (i) Sequence characteristics: (A) Length: 144 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:79: Val Lys Asp Ala Glu Glu Ala Val Arg He Ala Arg Glu He Gly Tyr 5 10 15 Pro Val Met He Lys Ala Ser Ala Gly Gly Gly Gly Lys Gly Met Arg 20 25 30 He Ala Trp Asp Asp Glu Glu Thr Arg Asp Gly Phe Arg Leu Ser Ser 35 40 45 Gin Glu Ala Ala Ser Ser Phe Gly Asp Asp Arg Leu Leu He Glu Lys 50 55 60 Phe He Asp Asn Pro Arg His He Glu He Gin Val Leu Gly Asp Lys 65 70 75 80 His Gly Asn Ala Leu Trp Leu Asn Glu Arg Glu Cys Ser He Gin Arg 85 90 95 Arg Asn Gin Lys Val Val Glu Glu Ala Pro Ser He Phe Leu Asp Ala 100 105 110 Glu Thr Arg Arg Ala Met Gly Glu Gin Ala Val Ala Leu Ala Arg Ala 115 120 125 Val Lys Tyr Ser Ser Ala Gly Thr Val Glu Phe Leu Val Asp Ser Lys 130 135 140 (2) INFORMATION FOR SEQ ID NO:80: (i) Sequence characteristics: (A) Length: 47 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:80: Lys Asn Phe Tyr Phe Leu Glu Met Asn Thr Arg Leu Gin Val Glu His 5 10 15 Pro Val Thr Glu Cys He His Trp Pro Gly Pro Ser Pro Gly Lys Thr 20 25 30 Val Leu Gin Glu His Leu Ser Gly Thr Asn Lys Leu He Phe Ala 35 40 45 (2) INFORMATION FOR SEQ ID NO:81: (i) Sequence characteristics: (A) Length: 29 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:81: Phe Asn Gly Trp Ala Val Glu Cys Arg Val Tyr Ala Glu Asp Pro Tyr 5 10 15 Lys Ser Phe Gly Leu Pro Ser He Gly Arg Leu Ser Gin 20 25 (2) INFORMATION FOR SEQ ID NO:82: (i) Sequence characteristics: (A) Length: 14 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:82: Tyr Gin Glu Pro Leu His Leu Pro Gly Val Arg Val Asp Ser 5 10 (2) INFORMATION FOR SEQ ID NO:83: (i) Sequence characteristics: (A) Length: 44 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:83: Gly He Gin Pro Gly Ser Asp He Ser He Tyr Tyr Asp Pro Met He 5 10 15 Ser Lys Leu He Thr Tyr Gly Ser Asp Arg Thr Glu Ala Leu Lys Arg 20 25 30 Met Ala Asp Ala Leu Asp Asn Tyr Val He Arg Gly 35 40 (2) INFORMATION FOR SEQ ID NO:84: (i) Sequence characteristics: (A) Length: 251 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:84: Val Thr His Asn He Ala Leu Leu Arg Glu Val He He Asn Ser Arg 5 10 15 Phe Val Lys Gly Asp He Ser Thr Lys Phe Leu Ser Asp Val Tyr Pro 20 25 30 Asp Gly Phe Lys Gly His Met Leu Thr Lys Ser Glu Lys Asn Gin Leu 35 40 45 Leu Ala He Ala Ser Ser Leu Phe Val Ala Phe Gin Leu Arg Ala Gin 50 55 60 His Phe Gin Glu Asn Ser Arg Met Pro Val He Lys Pro Asp He Ala 65 70 75 80 Asn Trp Glu Leu Ser Val Lys Leu His Asp Lys Val His Thr Val Val 85 90 95 Ala Ser Asn Asn Gly Ser Val Phe Ser Val Glu Val Asp Gly Ser Lys 100 105 110 Leu Asn Val Thr Ser Thr Trp Asn Leu Ala Ser Pro Leu Leu Ser Val 115 120 125 Ser Val Asp Gly Thr Gin Arg Thr Val Gin Cys Leu Ser Arg Glu Ala 130 135 140 Gly Gly Asn Met Ser He Gin Phe Leu Gly Thr Val Tyr Lys Val Asn 145 150 155 160 He Leu Thr Arg Leu Ala Ala Glu Leu Asn Lys Phe Met Leu Glu Lys 165 170 175 Val Thr Glu Asp Thr Ser Ser Val Leu Arg Ser Pro Met Pro Gly Val 180 185 190 Val Val Ala Val Ser Val Lys Pro Gly Asp Ala Val Ala Glu Gly Gin 195 200 205 Glu He Cys Val He Glu Ala Met Lys Met Gin Asn Ser Met Thr Ala 210 215 220 Gly Lys Thr Gly Thr Val Lys Ser Val His Cys Gin Ala Gly Asp Thr 225 230 235 240 Val Gly Glu Gly Asp Leu Leu Val Glu Leu Glu 245 250 (2) INFORMATION FOR SEQ ID NO:85: (i) Sequence characteristics: (A) Length: 90 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:85: Met Pro Tyr Arg Glu Arg Phe Cys Ala He Arg Trp Cys Arg Asn Ser 5 10 15 Gly Arg Ser Ser Gin Gin Leu Leu Trp Thr Leu Lys Arg Ala Pro Val 20 25 30 Tyr Ser Gin Gin Cys Leu Val Val Ser Arg Ser Leu Ser Ser Val Glu 35 40 45 Tyr Glu Pro Lys Glu Lys Thr Phe Asp Lys He Leu He Ala Asn Arg 50 55 60 Gly Glu He Ala Cys Arg Val He Lys Thr Cys Arg Lys Met Gly He 65 70 75 80 Arg Thr Val Ala He His Ser Asp Val Asp 85 90 (2) INFORMATION FOR SEQ ID NO:86: (i) Sequence characteristics: (A) Length: 21 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:86: Ala Ser Ser Val His Val Lys Met Ala Asp Glu Ala Val Cys Val Gly 5 10 15 Pro Ala Pro Thr Ser 20 (2) INFORMATION FOR SEQ ID NO:87: (i) Sequence characteristics: (A) Length: 38 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:87: Lys Ser Tyr Leu Asn Met Asp Ala He Met Glu Ala He Lys Lys Thr 5 10 15 Gly Ala Gin Ala Val His Pro Gly Tyr Gly Phe Leu Ser Glu Asn Lys 20 25 30 Glu Phe Ala Lys Cys Leu 35 (2) INFORMATION FOR SEQ ID NO:88: (i) Sequence characteristics: (A) Length: 41 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:88: Ala Ala Glu Asp Val Thr Phe He Gly Pro Asp Thr His Ala He Gin 5 10 15 Ala Met Gly Asp Lys He Glu Ser Lys Leu Leu Ala Lys Arg Ala Lys 20 25 30 Val Asn Thr He Pro Gly Phe Asp Gly 35 40 (2) INFORMATION FOR SEQ ID NO:89: (i) Sequence characteristics: (A) Length: 144 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:89: Leu Lys Asp Ala Asp Glu Ala Val Arg He Ala Arg Glu He Gly Tyr 5 10 15 Pro Val Met He Lys Ala Ser Ala Gly Gly Gly Gly Lys Gly Met Arg 20 25 30 He Pro Trp Asp Asp Glu Glu Thr Arg Asp Gly Phe Arg Phe Ser Ser 35 40 45 Gin Glu Ala Ala Ser Ser Phe Gly Asp Asp Arg Leu Leu He Glu Lys 50 55 60 Phe He Asp Asn Pro Arg His He Glu He Gin Val Leu Gly Asp Lys 65 70 75 80 His Gly Asn Ala Leu Trp Leu Asn Glu Arg Glu Cys Ser He Gin Arg 85 90 95 Arg Asn Gin Lys Val Val Glu Glu Ala Pro Ser He Phe Leu Asp Pro 100 105 110 Glu Thr Arg Arg Ala Met Gly Glu Gin Ala Val Ala* Trp Pro Lys Ala 115 120 125 Val Lys Tyr Ser Ser Ala Gly Thr Val Glu Phe Leu Val Asp Ser Gin 130 135 140 (2) INFORMATION FOR SEQ ID NO:90: (i) Sequence characteristics: (A) Length: 48 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:90: Lys Asn Phe Tyr Phe Leu Glu Met Asn Thr Arg Leu Gin Val Glu His 5 10 15 Pro Val Thr Glu Cys He Thr Gly Leu Asp Leu Val Gin Glu Met He 20 25 30 Leu Val Ala Lys Gly Tyr Pro Leu Arg His Lys Gin Glu Asp He Pro 35 40 45 (2) INFORMATION FOR SEQ ID NO:91: (i) Sequence characteristics: (A) Length: 29 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:91: He Ser Gly Trp Ala Val Glu Cys Arg Val Tyr Ala Glu Asp Pro Tyr 5 10 15 Lys Ser Phe Gly Leu Pro Ser He Gly Arg Leu Ser Gin 20 25 (2) INFORMATION FOR SEQ ID NO:92: (i) Sequence characteristics: (A) Length: 14 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:92: Tyr Gin Glu Pro He His Leu Pro Gly Val Arg Val Asp Ser 5 10 (2) INFORMATION FOR SEQ ID NO:93: (i) Sequence characteristics: (A) Length: 44 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:93: Gly He Gin Pro Gly Ser Asp He Ser He Tyr His Asp Pro Met He 5 10 15 Ser Lys Leu Val Thr Tyr Gly Ser Asp Arg Ala Glu Ala Leu Lys Arg 20 25 30 Met Glu Asp Ala Leu Asp Ser Tyr Val He Arg Gly 35 40 (2) INFORMATION FOR SEQ ID NO:94: (i) Sequence characteristics: (A) Length: 251 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:94: Val Thr His Asn He Pro Leu Leu Arg Glu Val He He Asn Thr Arg 5 10 15 Phe Val Lys Gly Asp He Ser Thr Lys Phe Leu Ser Asp Val Tyr Pro 20 25 30 Asp Gly Phe Lys Gly His Met Leu Thr Pro Ser Glu Arg Asp Gin Leu 35 40 45 Leu Ala He Ala Ser Ser Leu Phe Val Ala Ser Gin Leu Arg Ala Gin 50 55 60 Arg Phe Gin Glu His Ser Arg Val Pro Val He Arg Pro Asp Val Ala 65 70 75 80 Lys Trp Glu Leu Ser Val Lys Leu His Asp Glu Asp His Thr Val Val 85 90 95 Ala Ser Asn Asn Gly Pro Thr Phe Asn Val Glu Val Asp Gly Ser Lys 100 105 110 Leu Asn Val Thr Ser Thr Trp Asn Leu Ala Ser Pro Leu Leu Ser Val 115 120 125 Asn Val Asp Gly Thr Gin Arg Thr Val Gin Cys Leu Ser Pro Asp Ala 130 135 140 Gly Gly Asn Met Ser He Gin Phe Leu Gly Thr Val Tyr Lys Val His 145 150 155 160 He Leu Thr Lys Leu Ala Ala Glu Leu Asn Lys Phe Met Leu Glu Lys 165 170 175 Val Pro Lys Asp Thr Ser Ser Val Leu Arg Ser Pro Lys Pro Gly Val 180 185 190 Val Val Ala Val Ser Val Lys Pro Gly Asp Met Val Ala Glu Gly Gin 195 200 205 Glu He Cys Val He Glu Ala Met Lys Met Gin Asn Ser Met Thr Ala 210 215 220 Gly Lys Met Gly Lys Val Lys Leu Val His Cys Lys Ala Gly Asp Thr 225 230 235 240 Val Gly Glu Gly Asp Leu Leu Val Glu Leu Glu 245 250 (2) INFORMATION FOR SEQ ID NO:95: (i) Sequence characteristics: (A) Length: 17 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:95: Gin Arg Lys Phe Ala Gly Leu Arg Asp Asn Phe Asn Leu Leu Gly Glu 5 10 15 Lys (2) INFORMATION FOR SEQ ID NO:96: (i) Sequence characteristics: (A) Length: 34 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:96: Asn Lys He Leu Val Ala Asn Arg Gly Glu He Pro He Arg He Phe 5 10 15 Arg Thr Ala His Glu Leu Ser Met Gin Thr Val Ala He Tyr Ser His 20 25 30 Glu Asp (2) INFORMATION FOR SEQ ID NO:97: (i) Sequence characteristics: (A) Length: 24 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ϋ) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:97: Arg Leu Ser Thr His Lys Gin Lys Ala Asp Glu Ala Tyr Val He Gly 5 10 15 Glu Val Gly Gin Tyr Thr Pro Val 20 (2) INFORMATION FOR SEQ ID NO:98: (i) Sequence characteristics: (A) Length: 38 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:98: Gly Ala Tyr Leu Ala He Asp Glu He He Ser He Ala Gin Lys His 5 10 15 Gin Val Asp Phe He His Pro Gly Tyr Gly Phe Leu Ser Glu Asn Ser 20 25 30 Glu Phe Ala Asp Lys Val 35 (2) INFORMATION FOR SEQ ID NO:99: (i) Sequence characteristics: (A) Length: 41 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:99: Val Lys Ala Gly He Thr Trp He Gly Pro Pro Ala Glu Val He Asp 5 10 15 Ser Val Gly Asp Lys Val Ser Ala Arg Asn Leu Ala Ala Lys Ala Asn 20 25 30 Val Pro Thr Val Pro Gly Thr Pro Gly 35 40 (2) INFORMATION FOR SEQ ID NO:100: (i) Sequence characteristics: (A) Length: 144 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:100: He Glu Thr Val Glu Glu Ala Leu Asp Phe Val Asn Glu Tyr Gly Tyr 5 10 15 Pro Val He He Lys Ala Ala Phe Gly Gly Gly Gly Arg Gly Met Arg 20 25 30 Val Val Arg Glu Gly Asp Asp Val Ala Asp Ala Phe Gin Arg Ala Thr 35 40 45 Ser Glu Ala Arg Thr Ala Phe Gly Asn Gly Thr Cys Phe Val Glu Arg 50 55 60 Phe Leu Asp Lys Pro Lys His He Glu Val Gin Leu Leu Ala Asp Asn 65 70 75 80 His Gly Asn Val Val His Leu Phe Glu Arg Asp Cys Ser Val Gin Arg 85 90 95 Arg His Gin Lys Val Val Glu Val Ala Pro Ala Lys Thr Leu Pro Arg 100 105 110 Glu Val Arg Asp Ala He Leu Thr Asp Ala Val Lys Leu Ala Lys Glu 115 120 125 Cys Gly Tyr Arg Asn Ala Gly Thr Ala Glu Phe Leu Val Asp Asn Gin 130 135 140 (2) INFORMATION FOR SEQ ID NO:101: (i) Sequence characteristics: (A) Length: 51 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:101: Asn Arg His Tyr Phe He Glu He Asn Pro Arg He Gin Val Glu His 5 10 15 Thr He Thr Glu Glu He Thr Gly He Asp He Val Ala Ala Gin He 20 25 30 Gin He Ala Ala Gly Ala Ser Leu Pro Gin Leu Gly Leu Phe Gin Asp 35 40 45 Lys He Thr 50 (2) INFORMATION FOR SEQ ID NO:102: (i) Sequence characteristics: (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:102: Thr Arg Gly Phe Ala He Gin Cys Arg He Thr Thr Glu Asp Pro Ala 5 10 15 Lys Asn Phe Gin 20 (2) INFORMATION FOR SEQ ID NO:103: (i) Sequence characteristics: (A) Length: 14 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:103: Pro Asp Thr Gly Arg He Glu Val Tyr Arg Ser Ala Gly Gly 5 10 (2) INFORMATION FOR SEQ ID NO:104: (i) Sequence characteristics: (A) Length: 52 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:104: Asn Gly Val Arg Leu Asp Gly Gly Asn Ala Tyr Ala Gly Thr He He 5 10 15 Ser Pro His Tyr Asp Ser Met Leu Val Lys Cys Ser Cys Ser Gly Ser 20 30 Thr Tyr Glu He Val Arg Arg Lys Met He Arg Ala Leu He Glu Phe 35 40 45 Arg He Arg Gly 50 (2) INFORMATION FOR SEQ ID NO:105: (i) Sequence characteristics: (A) Length: 257 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:105: Val Lys Thr Asn He Pro Phe Leu Leu Thr Leu Leu Thr Asn Pro Val 5 10 15 Phe He Glu Gly Thr Tyr Trp Gly Thr Phe He Asp Asp Thr Pro Gin 20 25 30 Leu Phe Gin Met Val Ser Ser Gin Asn Arg Ala Gin Lys Leu Leu His 35 40 45 Tyr Leu Ala Asp Val Ala Asp Asn Gly Ser Ser He Lys Gly Gin He 50 55 60 Gly Leu Pro Lys Leu Lys Ser Asn Pro Ser Val Pro His Ser Tyr Asn 65 70 75 80 Met Tyr Pro Arg Val Tyr Glu Asp Phe Gin Lys Met Arg Glu Thr Tyr 85 90 95 Gly Asp Leu Ser Val Leu Pro Thr Arg Ser Phe Leu Ser Pro Leu Glu 100 105 110 Thr Asp Glu Glu He Glu Val Val He Glu Gin Gly Lys Thr Leu He 115 120 125 He Lys Leu Gin Ala Val Gly Asp Leu Asn Lys Lys Thr Gly Glu Arg 130 135 140 Glu Val Tyr Phe Asp Leu Asn Gly Glu Met Arg Lys He Arg Val Ala 145 150 155 160 Asp Arg Ser Gin Lys Val Glu Thr Val Thr Lys Ser Lys Ala Asp Met 165 170 175 His Asp Pro Leu His He Gly Ala Pro Met Ala Gly Val He Val Glu 180 185 190 Val Lys Val His Lys Gly Ser Leu He Lys Lys Gly Gin Pro Val Ala 195 200 205 Val Leu Ser Ala Met Lys Met Glu Met He He Ser Ser Pro Ser Asp 210 215 220 Gly Gin Val Lys Glu Val Phe Val Ser Asp Gly Glu Asn Val Asp Ser 225 230 235 240 Ser Asp Leu Leu Val Leu Leu Glu Asp Gin Val Pro Val Glu Thr Lys 245 250 255 Ala (2) INFORMATION FOR SEQ ID NO:106: (i) Sequence characteristics: (A) Length: 165 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:106: Val Leu Thr Val Ala Leu Phe Pro Gin Pro Gly Leu Lys Phe Leu Glu 5 10 15 Asn Arg His Asn Pro Ala Ala Phe Glu Pro Val Pro Gin Ala Glu Ala 20 25 30 Ala Gin Pro Val Ala Lys Ala Glu Lys Pro Ala Ala Ser Gly Val Tyr 35 40 45 Thr Val Glu Val Glu Gly Lys Ala Phe Val Val Lys Val Ser Asp Gly 50 55 60 Gly Asp Val Ser Gin Leu Thr Ala Ala Ala Pro Ala Pro Ala Pro Ala 65 70 75 80 Pro Ala Pro Ala Ser Ala Pro Ala Ala Ala Ala Pro Ala Gly Ala Gly 85 90 95 Thr Pro Val Thr Ala Pro Leu Ala Gly Thr He Trp Lys Val Leu Ala 100 105 110 Ser Glu Gly Gin Thr Val Ala Ala Gly Glu Val Leu Leu He Leu Glu 115 120 125 Ala Met Lys Met Glu Thr Glu He Arg Ala Ala Gin Ala Gly Thr Val 130 135 140 Arg Gly He Ala Val Lys Ala Gly Asp Ala Val Ala Val Gly Asp Thr 145 150 155 160 Leu Met Thr Leu Ala 165 (2) INFORMATION FOR SEQ ID NO:107: (i) Sequence characteristics: (A) Length: 123 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:107: Met Lys Leu Lys Val Thr Val Asn Gly Thr Ala Tyr Asp Val Asp Val 5 10 15 Asp Val Asp Lys Ser His Glu Asn Pro Met Gly Thr He Leu Phe Gly 20 25 30 Gly Gly Thr Gly Gly Ala Pro Ala Pro Arg Ala Ala Gly Gly Ala Gly 35 40 45 Ala Gly Lys Ala Gly Glu Gly Glu He Pro Ala Pro Leu Ala Gly Thr 50 55 60 Val Ser Lys He Leu Val Lys Glu Gly Asp Thr Val Lys Ala Gly Gin 65 70 75 80 Thr Val Leu Val Leu Glu Ala Met Lys Met Glu Thr Glu He Asn Ala 85 90 95 Pro Thr Asp Gly Lys Val Glu Lys Val Leu Val Lys Glu Arg Asp Ala 100 105 110 Val Gin Gly Gly Gin Gly Leu He Lys He Gly 115 120 (2) INFORMATION FOR SEQ ID NO:108: (i) Sequence characteristics: (A) Length: 1473 base pairs (B) Type: Nucleic acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Oligonucleotide (xi) Sequence Description: SEQ ID NO:108: GTGATGATCA AGGCATCATG GGGTGGGGGT GGTAAAGGAA TAAGGAAGGT ACATAATGAT 60 GATGAGGTCA GAGCATTGTT TAAGCAAGTG CAAGGAGAAG TCCCCGGATC GCCTATATTT 120 ATTATGAAGG TGGCATCTCA GAGTCGACAT CTAGAGGTTC AATTGCTCTG TGACAAGCAT 180 GGCAACGTGG CAGCACTGCA CAGTCGAGAC TGTAGTGTTC AAAGAAGGCA TCAAAAGATC 240 ATTGAGGAGG GACCAATTAC AGTTGCTCCT CCAGAAACAA TTAAAGAGCT TGAGCAGGCG 300 GCAAGGCGAC TAGCTAAATG TGTGCAATAT CAGGGTGCTG CTACAGTGGA ATATCTGTAC 360 AGCATGGAAA CAGGCGAATA CTATTTCCTG GAGCTTAATC CAAGGTTGCA GGTAGAACAC 420 CCTGTGACCG AATGGATTGC TGAAATAAAC TTACCYGCAT CTCAAGTTGT AGTAGGAATG 480 GGCATACCAC TCTACAACAT TCCAGAGATC AGACGCTTTT ATGGAATAGA ACATGGAGGT 540 GGCTATCAYG CTTGGAAGGA AATATCAGCT GTTGCAACTA AATTTGATYT GGACAAAGCA 600 CAGTCTGTAA AGCCAAARGG TCATTGTGTA GCAGTTAGAG TTACTAGCGA GGATCCAGAT 660 GATGGGTTTA AGCCTACMAG TGGAAGAGTR GAAGAGCTGA ACTTTAAAAG TAAACCCAAT 720 GTTTGGGCCT ATTTCTCYGT TARGTCCGGA GGTGCAATTC AYGAGTTCTC TGATTCCCAG 780 TTTGGTCATG TTTTTGCTTY TGGGGAATCT AGGTCWTTGG CAATAGCCAA TATGGTACTT 840 GGGTTAAAAG AGATCCAAAT TCGTGGAGAG ATACGCACTA ATGTTGACTA CACTGTGGAT 900 CTCTTGAATG CTGCAGAGTA CCGAGAAAAT AWGATTCACA CTGGTTGGCT AGACAGCAGA 960 ATAGCWATGC GYGTTAGAGC AGAGAGGCCC CCATGGTACC TTTCAGTTGT TGGTGGAGCT 1020 CTATATGAAG CATCAAGCAG GAGCTCGAGT GTTGTAACCG ATTATGTTGG TTATCTCAGT 1080 AAAGGTCAAA TACCACCAAA GCACATCTCT CTTGTCAAYT TGACTGTAAC ACTGAATATA 1140 GATGGGAGCA AATATACGAT TGAGACAGTA CGAGGTGGAC CCCGTAGCTA CAAATTAAGA 1200 ATTAATGAAT CAGAGGTTGA RGCAGAGATA CATTTCCTGC GAGATGGCGG ACYCTTAATG 1260 CAGTYGGATG GAAACAGTCA TGTAATTTAC GCCGAGACAG AAGCTKCTGG CACGCGCCTT 1320 CTAATCAATG GGAGAACATG CTTATTACAG AAAGAGCAYG ATCCTTCCAG GTTGTTGGCT 1380 GATACACCRT GCAARCTTCT TCGGTTTTTG GTCGCGGATR GTTCTCATGT GGTTGCTGAT 1440 ACGCCATATG CYGAGGTGGA GGCCATGAAA ATG 1473 (2) INFORMATION FOR SEQ ID NO:109: (i) Sequence characteristics: (A) Length: 491 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (ix) Features (A) NAME/KEY: Xaa (B) LOCATION: 248, 267, 311, 412, 418, 422, 436, and 474 (C) IDENTIFICATION METHOD: Xaa = any amino acid (xi) Sequence Description: SEQ ID NO:109: Val Met He Lys Ala Ser Trp Gly Gly Gly Gly Lys Gly He Arg Lys 5 10 15 Val His Asn Asp Asp Glu Val Arg Ala Leu Phe Lys Gin Val Gin Gly 20 25 30 Glu Val Pro Gly Ser Pro He Phe He Met Lys Val Ala Ser Gin Ser 35 40 45 Arg His Leu Glu Val Gin Leu Leu Cys Asp Lys His Gly Asn Val Ala 50 55 60 Ala Leu His Ser Arg Asp Cys Ser Val Gin Arg Arg His Gin Lys He 65 70 75 80 He Glu Glu Gly Pro He Thr Val Ala Pro Pro Glu Thr He Lys Glu 85 90 95 Leu Glu Gin Ala Ala Arg Arg Leu Ala Lys Cys Val Gin Tyr Gin Gly 100 105 110 Ala Ala Thr Val Glu Tyr Leu Tyr Ser Met Glu Thr Gly Glu Tyr Tyr 115 120 125 Phe Leu Glu Leu Asn Pro Arg Leu Gin Val Glu His Pro Val Thr Glu 130 135 140 Trp He Ala Glu He Asn Leu Pro Ala Ser Gin Val Val Val Gly Met 145 150 155 160 Gly He Pro Leu Tyr Asn He Pro Glu He Arg Arg Phe Tyr Gly He 165 170 175 Glu His Gly Gly Gly Tyr His Ala Trp Lys Glu He Ser Ala Val Ala 180 185 190 Thr Lys Phe Asp Leu Asp Lys Ala Gin Ser Val Lys Pro Lys Gly His 195 200 205 Cys Val Ala Val Arg Val Thr Ser Glu Asp Pro Asp Asp Gly Phe Lys 210 215 220 Pro Thr Ser Gly Arg Val Glu Glu Leu Asn Phe Lys Ser Lys Pro Asn 225 230 235 240 Val Trp Ala Tyr Phe Ser Val Xaa Ser Gly Gly Ala He His Glu Phe 245 250 255 Ser Asp Ser Gin Phe Gly His Val Phe Ala Xaa Gly Glu Ser Arg Ser 260 265 270 Leu Ala He Ala Asn Met Val Leu Gly Leu Lys Glu He Gin He Arg 275 280 285 Gly Glu He Arg Thr Asn Val Asp Tyr Thr Val Asp Leu Leu Asn Ala 290 295 300 Ala Glu Tyr Arg Glu Asn Xaa He His Thr Gly Trp Leu Asp Ser Arg 305 310 315 320 He Ala Met Arg Val Arg Ala Glu Arg Pro Pro Trp Tyr Leu Ser Val 325 330 335 Val Gly Gly Ala Leu Tyr Glu Ala Ser Ser Arg Ser Ser Ser Val Val 340 345 350 Thr Asp Tyr Val Gly Tyr Leu Ser Lys Gly Gin He Pro Pro Lys His 355 360 365 He Ser Leu Val Asn Leu Thr Val Thr Leu Asn He Asp Gly Ser Lys 370 375 380 Tyr Thr He Glu Thr Val Arg Gly Gly Pro Arg Ser Tyr Lys Leu Arg 385 390 395 400 He Asn Glu Ser Glu Val Glu Ala Glu He His Xaa Leu Arg Asp Gly 405 410 415 Gly Xaa Leu Met Gin Xaa Asp Gly Asn Ser His Val He Tyr Ala Glu 420 425 430 Thr Glu Ala Xaa Gly Thr Arg Leu Leu He Asn Gly Arg Thr Cys Leu 435 440 445 Leu Gin Lys Glu His Asp Pro Ser Arg Leu Leu Ala Asp Thr Pro Cys 450 455 460 Lys Leu Leu Arg Phe Leu Val Ala Asp Xaa Ser His Val Val Ala Asp 465 470 475 480 Thr Pro Tyr Ala Glu Val Glu Ala Met Lys Met 485 490 (2) INFORMATION FOR SEQ ID NO:110: (i) Sequence characteristics: (A) Length: 436 base pairs (B) Type: Nucleic acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Oligonucleotide (xi) Sequence Description: SEQ ID NO:110: TCTAGACTTT AACGAGATTC GTCAACTGCT GACAACTATT GCACAAACAG ATATCGCGGA 60 AGTAACGCTC AAAAGTGATG ATTTTGAACT AACGGTGCGT AAAGCTGTTG GTGTGAATAA 120 TAGTGTTGTG CCGGTTGTGA CAGCACCCTT GAGTGGTGTG GTAGGTTCGG GATTGCCATC 180 GGCTATACCG ATTGTAGCCC ATGCTGCCCA ATCTCCATCT CCAGAGCCGG GAACAAGCCG 240 TGCTGCTGAT CATGCTGTCA CGAGTTCTGG CTCACAGCCA GGAGCAAAAA TCATTGACCA 300 AAAATTAGCA GAAGTGGCTT CCCCAATGGT GGGAACATTT TACCGCGCTC CTGCACCAGG 360 TGAAGCGGTA TTTGTGGAAG TCGGCGATCG CATCCGTCAA GGTCAAACCG TCTGCATCAT 420 CGAAGCGATG AAAAUG 436 114 (2) INFORMATION FOR SEQ ID NO: 111: (i) Sequence characteristics: (A) Length: 145 amino acids (B) Type: Amino acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Peptide (xi) Sequence Description: SEQ ID NO:111: Leu Asp Phe Asn Glu He Arg Gin Leu Leu Thr Thr He Ala Gin Thr 5 10 15 Asp He Ala Glu Val Thr Leu Lys Ser Asp Asp Phe Glu Leu Thr Val 20 25 30 Arg Lys Ala Val Gly Val Asn Asn Ser Val Val Pro Val Val Thr Ala 35 40 45 Pro Leu Ser Gly Val Val Gly Ser Gly Leu Pro Ser Ala He Pro He 50 55 60 Val Ala His Ala Ala Pro Ser Pro Ser Pro Glu Pro Gly Thr Ser Arg 65 70 75 80 Ala Ala Asp His Ala Val Thr Ser Ser Gly Ser Gin Pro Gly Ala Lys 85 90 95 He He Asp Gin Lys Leu Ala Glu Val Ala Ser Pro Met Val Gly Thr 100 105 110 Phe Tyr Arg Ala Pro Ala Pro Gly Glu Ala Val Phe Val Glu Val Gly 115 120 125 Asp Arg He Arg Gin Gly Gin Thr Val Cys He He Glu Ala Met Lys 130 135 140 Met 145 (2) INFORMATION FOR SEQ ID NO:112: (i) Sequence characteristics: (ii) Molecule type: Oligonucleotide (ix) Features (A) NAME/KEY: N (B) LOCATION: 11, 14 (C) IDENTIFICATION METHOD: N = A, G, C, T (xi) Sequence Description: SEQ ID NO:112: TCGAATTCGT NATNATHAAR GC 22 (2) INFORMATION FOR SEQ ID NO:113: (i) Sequence characteristics: (ii) Molecule type: Oligonucleotide (ix) Features (A) NAME/KEY: N (B) LOCATION: 17 (C) IDENTIFICATION METHOD: N = A, G, C, T (xi) Sequence Description: SEQ ID NO:113: GCTCTAGAGK RTGYTCNACY TC 22 (2) INFORMATION FOR SEQ ID NO:114: (i) Sequence characteristics: (A) Length: 21 base pairs (B) Type: Nucleic acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Oligonucleotide (xi) Sequence Description: SEQ ID NO:114: GCTCTAGAAT ACTATTTCCT G 21 (2) INFORMATION FOR SEQ ID NO:115: (i) Sequence characteristics: (A) Length: 22 base pairs (B) Type: Nucleic acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Oligonucleotide (ix) Features (A) NAME/KEY: N (B) LOCATION: 10, 20 (C) IDENTIFICATION METHOD: N = A, G, C, T (xi) Sequence Description: SEQ ID NO:115: TCGAATTCWN CATYTTCATN RC 22 (2) INFORMATION FOR SEQ ID NO:116: (i) Sequence characteristics: (A) Length: 23 base pairs (B) Type: Nucleic acid (C) Strandedness: Single (D) Topology: Linear (ii) Molecule type: Oligonucleotide (xi) Sequence Description: SEQ ID NO:116: GCTCTAGAYT TYAAYGARAT HMG 23

Claims: WHAT IS CLAIMED IS: 1. An isolated and purified polynucleotide of from about 1350 to about 40,000 base pairs that encodes a polypeptide having the ability to catalyze the carboxylation of a biotin carboxyl carrier protein of a cyanobacterium. 2. The polynucleotide according to claim 1 wherein said polypeptide is a subunit of acetyl-CoA carboxylase and participates in the carboxylation of acetyl-CoA. 3. The polynucleotide according to claim 1 wherein said cyanobacterium is Anabaena or Synechococcus. 4. The polynucleotide according to claim 3 wherein said biotin carboxyl carrier protein includes the amino acid residue sequence shown in SEQ ID NO: 111 or a functional equivalent thereof. 5. The polynucleotide according to claim 1 wherein said polypeptide has the amino acid residue sequence of Figure 1 or Figure 2. 6. The polynucleotide according to claim 1 that includes (a) the DNA sequence of SEQ ID NO: l from about nucleotide position 1300 to about nucleotide position 2650; (b) the DNA sequence of SEQ ID NO: 1 ; or (c) the DNA sequence of SEQ ID NO:5. 7. An isolated and purified polynucleotide of from about 480 to about 40,000 base pairs that encodes a biotin carboxyl carrier protein of a cyanobacterium. 8. The polynucleotide according to claim 7 wherein said cyanobacterium is Anabaena. 9. The polynucleotide according to claim 8 wherein said biotin carboxyl carrier protein includes the amino acid residue sequence of SEQ ID NO: 111 or a functional equivalent thereof. 10. The polynucleotide according to claim 7 that includes the DNA sequence of SEQ ID NO: 110. 11. An isolated and purified DNA molecule comprising a promoter operatively linked to a coding region that encodes a polypeptide having the ability to catalyze the carboxylation of a biotin carboxyl carrier protein of a cyanobacterium, which coding region is operatively linked to a transcription-terminating region, whereby said promoter drives the transcription of said coding region. 12. An isolated and purified DNA molecule comprising a promoter operatively linked to an coding region that encodes a biotin carboxyl carrier protein of a cyanobacterium. 13. An isolated and purified polynucleotide of from about 1500 to about 150,000 base pairs that encodes a plant polypeptide having the ability to catalyze the carboxylation of acetyl-CoA. 14. The polynucleotide according to claim 13 wherein said plant polypeptide is a monocotyledonous plant polypeptide. 15. The polynucleotide according to claim 14 wherein said monocotyledonous plant is wheat, rice, maize, barley, rye, oats or timothy grass. 16. The polynucleotide according to claim 13 wherein said plant polypeptide is a dicotyledonous plant polypeptide. 17. The polynucleotide according to claim 16 wherein said dicotyledonous plant is soybean, rape, sunflower, tobacco, Arabidopsis, petunia, canola, pea, bean, tomato, potato, lettuce, spinach, canot, canola, alfalfa, or cotton. 18. The polynucleotide according to claim 13 wherein said plant polypeptide includes the amino acid residue sequence of SEQ ID NO: 109. 19. The polynucleotide according to claim 13 that includes the nucleotide sequence of SEQ ID NO:7. 20. An isolated polypeptide having the ability to catalyze the carboxylation of a biotin carboxyl carrier protein of a cyanobacterium. 21. The polypeptide according to claim 20 wherein said cyanobacterium is Anabaena or Synechococcus. 22. The polypeptide according to claim 20 wherein said biotin carboxyl carrier protein includes the amino acid sequence of SEQ ID NO: ll l. 23. The polypeptide according to claim 20 having the amino acid residue sequence of Figure 1 or Figure 2. 24. An isolated and purified biotin carboxyl carrier protein of a cyanobacterium. 25. The protein according to claim 24 wherein said cyanobacterium is Anabaena. 26. The protein according to claim 25 including the amino acid residue sequence of SEQ ID NO: 111. 27. An isolated and purified plant polypeptide having a molecular weight of about 220 KD, di ers of which have the ability to catalyze the carboxylation of acetyl-CoA. 28. A process of increasing the herbicide resistance of a monocotyledonous plant comprising transforming said plant with a DNA molecule comprising a promoter operatively linked to a coding region that encodes a herbicide resistant polypeptide having the ability to catalyze the carboxylation of acetyl-CoA, which coding region is operatively linked to a transcription-terminating region, whereby said promoter is capable of driving the transcription of said coding region in a monocotyledonous plant. 29. The process according to claim 28 wherein said polypeptide is an acetyl-CoA carboxylase enzyme. 30. The process ccording to claim 29 wherein said acetyl- CoA carboxylase is a dicotyledonous plant acetyl-CoA carboxylase enzyme. 31. The process according to claim 30 wherein said coding region includes the DNA sequence of SEQ ID NO: 108. 32. The process according to claim 28 wherein said promoter is CaMV35. 33. A transformed plant produced in accordance with the process of claim 28. 34. A transgenic plant having incorporated into its genome a transgene that encodes a dicotyledonous polypeptide having the ability to catalyze the carboxylation of acetyl-CoA. 35. A process of altering the carboxylation of acetyl-CoA in a cell comprising transforming said cell with a DNA molecule comprising a promoter operatively linked to a coding region that encodes a plant polypeptide having the ability to catalyze the carboxylation of acetyl-CoA, which coding region is operatively linked to a transcription-terminating region, whereby said promoter is capable of driving the transcription of said coding region in said cell. 36. The process according to claim 35 wherein said cell is a cyanobacterium or a plant cell. 37. The process according to claim 35 wherein said plant polypeptide is a plant acetyl-CoA carboxylase enzyme. 38. The process according to claim 37 wherein said plant acetyl-CoA carboxylase enzyme is a monocotyledonous plant acetyl-CoA carboxylase enzyme. 39. The process according to claim 38 wherein said monocotyledonous plant acetyl-CoA carboxylase enzyme is wheat acetyl- CoA carboxylase enzyme. 40. A transformed cyanobacterium produced in accordance with the process of claim 36. 41. A process for determining the inheritance of plant resistance to herbicides of the aryloxyphenocypropionate or cyclohexanedione class, which process comprises the steps of: (a) measuring resistance to herbicides of the aryloxyphenocypropionate or cyclohexanedione class in a parental plant line and in progeny of said parental plant line; (b) purifying DNA from said parental plant line and said progeny; (c) digesting said DNA with restriction enzymes to form DNA fragments; (d) fractionating said fragments on a gel; (e) transferring said fragments to a filter support; (f) annealing said fragments with a labelled RFLP probe consisting of a DNA molecule that encodes acetyl-CoA carboxylase or a portion thereof; and (g) detecting the presence of complexes between said fragments and said RFLP probe; and (h) conelating the herbicide resistance of step (a) with the complexes of step (g) and thereby the inheritance of herbicide resistance. 42. The process according to claim 41 wherein said acetyl- CoA carboxylase is a dicotyledonous plant acetyl-CoA carboxylase enzyme. 43. The process according to claim 41 wherein said acetyl- CoA carboxylase is a mutated monocotyledonous plant acetyl-CoA carboxylase that confers herbicide resistance or a hybrid acetyl-CoA carboxylase comprising a portion of a dicotyledonous plant acetyl-CoA carboxylase, a portion of a dicotyledonous plant acetyl-CoA carboxylase or one or more domains of a cyanobacterial acetyl-CoA carboxylase. 44. A process for identifying herbicide resistant variants of a plant acetyl-CoA carboxylase comprising the steps of: (a) transforming cyanobacteria with a DNA molecule that encodes a monocotyledonous plant acetyl-CoA carboxylase enzyme to form transformed cyanobacteria; (b) inactivating cyanobacterial acetyl-CoA carboxylase; (c) exposing said transformed cyanobacteria to a herbicide that inhibits acetyl-CoA carboxylase activity; (d) identifying transformed cyanobacteria that are resistant to said herbicide; and (e) characterizing DNA that encodes acetyl-CoA carboxylase from the cyanobacteria of step (d).

Inventors: GORNICKI PIOTR, HASELKORN ROBERT, GORNICKI, PIOTR, HASELKORN, ROBERT
Applicants: ARCH DEV CORP, ARCH DEVELOPMENT CORPORATION
Application year: 1993
Main classification: C12N15
IPC codes: C12N1, C12N9, C12N15