PLANT PATHOGEN RESPONSE GENE

Abstract: DNA molecules encoding a family of zinc-finger DNA binding domains, which appears to function to monitor levels of a superoxide-dependent signal and negatively regulates a plant cell death pathway, including wild-type LSD1, LOL1 and LOL2, and proteins which physically interact with LSD1, indicating a function with LSD1 of controlling plant cells' response to pathogens.

Description: PLANT PATHOGEN RESPONSE GENE CROSS-REFERENCE TO RELATED APPLICATIONS This application claims benefit of U.S. Provisional Application No. 60/039,063 filed February 28, 1997. BACKGROUND OF THE INVENTION Field of the Invention This invention relates to a novel DNA molecule that encodes a novel polypeptide, LSDl, which has an effect in regulating the initial response of plants to pathogens and the subsequent spread of plant cell death engendered by infection, the protein encoded by the gene, and transgenic plants comprising the DNA molecule. This invention also relates to novel DNA molecules encoding LSDl related proteins LOLl and LOL2. In addition, it relates to novel DNA molecules encoding proteins which directly interact with LSDl . Description of the Related Art Controlled induction of cell death occurs during both normal plant development and as the rapid, localized response to pathogen infection known as the hypersensitive response (HR) (Stakman, 1915; Goodman and Novacky, 1994; Dangl et al., 1996). The HR is a feature of most, but not all, disease resistance reactions in plants. The disclosure of these publications and all others cited herein, as well as of the priority application, is incorporated herein by reference. Genetic control of disease resistance reactions is of two broad classes. The first is determined by specific interactions between particular alleles of pathogen avr (avirulence) gene loci and an allele of the corresponding plant disease resistance (R ) locus. When these alleles are present in both host and pathogen, the result is disease resistance in the plant, and the interaction is said to be "incompatible". If either the plant R allele or the cognate pathogen avr gene are absent or inactive, disease results and the interaction in said to be "compatible" (reviewed by Flor, 1971; Crute, 1985; Keen, 1990; Pryor and Ellis, 1993). A great deal of progress has been made recently in understanding the molecular structure of R genes and their predicted products (reviewed by Dangl, 1995; Staskawicz et al, 1995; Bent, 1996). These molecules function to recognize avr dependent signals and trigger the plant cell to begin the chain of signal transduction events culminating in a halt of pathogen growth. The simplest mechanistic interpretation of allele-specific disease resistance is that the R gene product recognizes the avr gene product directly. Although no direct avr-R protein interaction has been shown in planta, expression of avr genes in plant cells can be sufficient to trigger the HR in a ^-dependent manner, and avr-R protein-protein interactions can occur in yeast two-hybrid systems (Gopalan et al., 1996; Scofield et al., 1996; Tang et al, 1996). The second mode of genetic control of disease resistance is termed "non-host" resistance and describes in essence those interactions which lack genetic variability in either host or pathogen such that no virulent pathogen and no susceptible host line have been identified. While it is not beyond reason to assume that traditional "non-host" interactions are simply a series of allele specific recognition events occurring simultaneously (Whalen et al., 1988; Kobayashi et al., 1989; Valent et al., 1990), it is also possible that this mode of resistance is mechanistically distinct from that mediated by allele-specific interactions. Pathogen ligands (termed elicitors) which mediate several key non-host interactions have been isolated, although their corresponding plant receptors have not (Cosio, et al. 1992; Nϋrnberger et al, 1994). Subsequent to pathogen recognition by either of these two systems, the plant cell deploys a battery of inducible defense responses. Chief among the earliest events are + + calcium influx, K -H exchange leading to alkalinization of the extracellular space, and an oxidative burst (reviewed in Godiard et al., 1994; Hammond-Kosack and Jones, 1996). The latter is potentially mediated by a plasma membrane NADPH oxidase analogous to that used by mammalian neutrophils (Low and Merida, 1996), although other models exist (Bolwell et al., 1995). Parts of this cascade are linearly regulated in at least some systems: 2+ blocking of Ca influx blocks anion channel activity, the oxidative burst and downstream events including cell death; blocking anion channels effects only ROI production and 2+ defense gene activation, but not Ca influx (Nϋrnberger et al., 1994; Levine et al., 1996; May et al., 1996). Consequent production of reactive oxygen intermediates (ROI) occurs with kinetics and magnitude suggesting a key role in either pathogen elimination, subsequent signaling of downstream effector functions, or both (reviewed by Baker and Orlandi, 1995; Low and Merida, 1996). H2O2 can have a key role in resistance responses, and cell wall strengthening (Brisson et al., 1994; Levine et al., 1994; Levine et al., 1996), and superoxide produced as the proximal ROI in the burst has also been implicated in initiating HR (Doke, 1983; Jabs et al., 1996). Transcription and translation of plant genes are required for HR. These signals are thought to culminate in transcriptional activation of a variety of plant genes, HR, and the production of both local and systemic signals that protect the plant from further infection. It is unclear whether these effector functions are controlled by linear, interdigitating, or bifurcating signal pathways. Cell death during the HR may be a direct consequence of ROI toxicity, or it may be a secondary consequence of signals derived from ROI. It is not known whether HR is required to halt pathogen growth. Nonetheless, HR is correlated with the onset of systemic acquired resistance (SAR) to secondary infection in distal tissue (reviewed by Ryals et al., 1996). In at least tobacco and Arabidopsis, enzymatic blocking of salicylic acid (SA) accumulation subsequent to infection alters disease resistance responses, and SA in distal tissues is required for SAR (Gaffney et al., 1993; Delaney et al., 1994; Vernooij et al., 1994). SA accumulates following the oxidative burst to high levels locally at infection sites. The biochemical properties of SA as an inhibitor of a variety of enzymes suggest a model whereby SA or a radical derived from it poisons the infected cell, causing its death (Enyedi et al., 1992; Malamy et al., 1992; Chen et al., 1994; Durner and Klessig, 1995; Rueffler et al., 1995). Recent descriptions of the morphology of cell death during infection suggest, in at least some cases, parallels with animal apoptosis (Mittler et al., 1995; Kosslak et al., 1996; Levine et al., 1996; Ryerson and Heath, 1996; Wang et al, 1996a; reviewed by Dangl et al., 1996). A molecular understanding of both the signaling events that control the onset of this specialized plant cell death and the mechanisms by which these cells die will hasten approaches to manipulate cell death to protect plants from disease. A number of researchers have isolated mutants in Arabidopsis which exhibit constitutive onset of HR-like cell death in the absence of pathogen (Greenberg and Ausubel, 1993; Dietrich et al., 1994; Greenberg et al, 1994). These mutants resemble a variety of mutants in crop species isolated since the 1920s and broadly categorized as "lesion mimic mutations" (Langford, 1948; Kiyosawa, 1970; Walbot et al., 1983; Johal et al., 1994). A series of non-allelic mutations was isolated which expressed histochemical and molecular markers associated with disease resistance responses. These mutants subdivide the lesion mimic class into a "lesions simulating disease resistance" or Isd phenotype (Dietrich et al., 1994). These mutants also exhibited heightened resistance to otherwise virulent bacterial and oomycete pathogens when lesions were present, demonstrating that these cell death phenotypes can trigger pathogen non-specific resistance resembling SAR. Similar "accelerated cell death" or acd mutants have been described by Greenberg and Ausubel (Greenberg et al., 1994). Greenberg and Ausubel (1993) additionally isolated a mutant which though expressing an acd phenotype was in fact more susceptible to pathogen. It is thus possible to identify genetically at least two types of cell death, namely those which feed into a pathway culminating in establishment of a disease resistant state, and those which do not. The Isdl mutant is exceptional. In conditions permissive for wild type plant growth and in the absence of detectable microscopic lesions, the Isdl mutant is hyper-responsive to challenge by a variety of stimuli including pathogens and low doses of chemicals which trigger the onset of SAR (Dietrich et al, 1994). Mutant Isdl plants are resistant to otherwise virulent pathogens in conditions where no spontaneous cell death lesions form. Following initiation of cell death in a local spot on a leaf, lesions propagate throughout the leaf and kill it 2-4 days later. Propagation of locally initiated cell death is confined to the inoculated leaf. Thus, LSDl functions to negatively regulate both the initial response to pathogens and the subsequent spread of cell death. Superoxide is a necessary and sufficient trigger for this phenotype, and superoxide production precedes onset of cell death by 8-16 hours following initiation by three different triggers (Jabs et al., 1996). Therefore, the LSDl gene responds to either superoxide or to a signal derived from it to down regulate or dampen the cell death response, resulting in the typical locally bounded HR. The invention herein includes the LSDl gene, which encodes the first member of a new subclass of zinc- finger proteins in Arabidopsis. It is therefore an object of the invention to provide a novel DNA molecule, LSDl, isolated from Arabidopsis which works to protect plant cells in response to pathogens, and DNA molecules encoding LSDl related proteins LOLl and LOL2. It is a further object of the invention to provide the protein encoded by LSDl, and transgenic plants comprising LSDl. Knowledge of the structure of the LSDl gene allows accurate creation of particular mutants (e.g., deletion and point mutations), for example, mutants having a dominant negative phenotype, analogous to the mutants of Drosophila PANNIER gene (Ramain et al., 1993), using methods known in the art. This in turn allows engineering of transgenic crop plants which do not suffer cell death, but are still resistant to infection. In addition, expression of the dominant negative LSDl protein may be refined so that it is expressed very quickly after infection. The LSDl protein is also a useful target for herbicide development. Transgenic plants may be made in which LSDl mutant genes are expressed which are resistant to herbicidal compounds which normally result in cell death in combination with the wild-type LSDl. Mutants of the LSDl gene are tested in a Isdl background to determine if the mutant has a normal or novel function, and in a wild-type background to determine the existence of a dominant negative function. Other objects and advantages will be more fully apparent from the following disclosure and appended claims. SUMMARY OF THE INVENTION The invention herein comprises the DNA molecule of the wild-type LSDl, which functions to monitor levels of a superoxide-dependent signal and negatively regulates a plant cell death pathway. The predicted LSDl protein contains three zinc-finger domains, defined by CxxCxRxxLMYxxGASxVxCxxC (SEQ ID NO.54). The invention further comprises a protein encoded by LSDl, and transgenic plants comprising LSDl, and mutations thereof. In particular, the preferred embodiments of the invention herein include the following: an isolated DNA molecule, encoding the LSDl polypeptide sequence, selected from the group consisting of SEQ ID NOS: 13- 15; the LSDl DNA molecule having the nucleotide sequence as set forth in SEQ ID NO: 13; the DNA molecule that is cDNA; the DNA molecule which is genomic DNA; a chimeric construction comprising a promoter sequence and the LSDl DNA molecule or portions of the LSDl DNA molecule; a recombinant plant transformed with the LSDl DNA molecule; a transformed plant comprising a DNA molecule encoding a protein as set out in SEQ ID NO: 16 or SEQ ID NO:17; an isolated protein molecule comprising the protein set out in SEQ ID NO:16 or SEQ ID NO:17; a transformation vector comprising a LSDl DNA molecule as set forth herein; an isolated DNA molecule encoding the zinc finger consensus sequence shown in SEQ ID NOS: 1-3; and anything that hybridizes to the LSDl DNA molecule set forth herein under hybridization conditions as defined herein. Other objects and features of the inventions will be more fully apparent from the following disclosure and appended claims. BRIEF DESCRIPTION OF THE DRAWINGS Figures 1A-C show the physical delineation of the Isdl mutation. Figure 1A shows YAC clones at Isdl. The arrowheads imply the YAC clone extending in the direction given, solid vertical black bars denote YAC ends used to isolate genomic phage clones and subsequently converted into CAPS RFLP markers as described (refer to Figure 2 for their map position and to Tables 1 and 2, Examples II and III, for their definition). Figure IB shows the three BAC clones which contained the CAPS markers listed above BAC1G5. The arrowheads imply extension of the BAC clone in the direction shown. The scale in Figures 1A and IB are the same. Figure 1C shows the genomic phage clones positioned under an expansion of three of the BACs. The diamond-filled bar represents the 8A6-1.3 clone, which co-segregated with Isdl, used to isolate these phage. The Isdl deletion is noted at the bottom. Figure 2 is a genetic linkage map of the Isdl region. The vertical line at the left represents the section of Arabidopsis chromosome 4 between CH42 and B9-1.8 (telomeric toward bottom). CAPS-based RFLP markers discussed in the text intersect the chromosome, and their relative recombination frequencies in the F mapping population are placed in the center. The number of meioses identified among the total number of F 's scored is at the right. The arrowhead denotes the co-segregating marker. Figures 3A-C show molecular fine mapping of the Isdl locus. Figures 3A and 3B show genomic DNA blots demonstrating the presence of a 0.8 kb deletion om the Isdl mutant. Genomic DNA (5 g) from wild type Ws-0 or Isdl was digested with (for each pair of lanes from left to right) EcoRI, Hindlll, a double digest of Hindlll and Xbal. or Kpnl. In Figure 3A, the blot was probed with the 0.8 kb EcoRI-Xbal. In Figure 3B, a duplicate blot was probed with the 4.5 kb Pstl-Xhol fragment. The probes are depicted in Figure 3C, and were isolated from phage clones depicted in Figure lC. Molecular weight markers are the Gibco-BRl 1 kb ladder. Figure 3C shows the restriction map in and around the Isdlgene. The extent of the deletion of this locus is shown as are the extent of the hybridization of the various restriction fragments with Isdl cDNAs. Genomic restriction fragments used in complementation experiments are underlined. The asterisk refers to an Xhol site derived from the phage lambda cloning junction. Figure 4 shows that the Isdl mutation is an mRNA null allele. RNA blots (1 g of polyA+ RNA) from leaf tissue of 5 week old plants kept in short days (permissive for Isdl growth) 3 days after spraying with either IN A (0.3 mg/ml powder containing 25% active ingredient, or 4 mM), or wettable powder control. Spreading Isdl lesions had just started to appear at the time of leaf harvest. Probes were purified inserts from the LSDl cDNA as represented by EST 82D11T7 (top), a PR-1 cDNA (Uknes et al, 1993b), and an actin cDNA. The blot was probed successively in the order displayed. Figure 5 shows the zinc finger domains (SEQ ID NOS:l-3) of the predicted LSDl protein and the alignment of the three zinc finger domains. The numbers at the left and right refer to amino acid residue position in the deduced LSDl protein. Vertical lines indicate conservation in pairwise comparison, and a colon indicates conservative substitution. A consensus sequence is listed below, with conservative substitutions noted in the second line of consensus where "+" is basic, plus charged; and "@" is amide, polar, uncharged, hydrophilic. Figure 6 shows how the carboxyl portion of the deduced LSDl protein is related to known DNA-binding and transcription factors. Vertical lines indicate conservation in pairwise comparison, and a colon indicates conservative substitution. Figure 6A shows homology of a slightly longer portion of the deduced LSDl protein with mammalian insulin receptor substrate proteins. The LSDl translation product (SEQ ID NO:4) is shown on the top, aligned with the mouse insulin receptor substrate (SEQ ID NO:5). In this region, all mammalian insulin receptor substrates are identical. Figure 6B shows the homology of LSDl, on each top line, with four known transcription factors. The LSDl translation product (SEQ ID NO:6) is shown on top, and below it are the related domains from a human early growth response (EGR) Zn-fmger protein (SEQ ID NO: 7, a human TGF —early induced Zn-fmger protein (SEQ ID NO: 8), a Xenopus laevis H-L-H transcription factor (SEQ ID NO:9), and the human ELK-1 protein (SEQ ID NO: 10). Figure 6C shows the homology of a LSDl transcription product (SEQ ID NO: 11) with a putative maize transcription initiator binding protein (SEQ ID NO: 12). GenBank accession numbers of each protein are listed at the right. Figure 7 shows the consensus sequence of the zinc finger domains (SEQ ID NOS:63-65, respectively) of LSDl (A), LOLl (B) and LOL2 (C). Figure 8 shows the homologies between the first (A), second (B) and third (C) zinc finger domains of LSDl, LOLl and LOL2 DETAILED DESCRIPTION OF THE INVENTION AND PREFERRED EMBODIMENTS THEREOF The present invention provides a genomic DNA sequence (SEQ ID NO: 13) and a cDNA sequence (SEQ ID NOS: 14- 15) or the LSDl gene which is required for the regulation of initial plant response to pathogens, and cDNA proteins deduced (from short form, MG7-SEQ ID NO: 16; from long form, MG, SEQ ID NO: 17). In addition, the invention herein provides functional protein domain sequences involved in regulating genes controlling cell death. Gene expression can be regulated by attaching a promoter to the LSDl gene, which may be either the native promoter or any other promoter. The invention herein includes the DNA molecule having the nucleotide sequence as set forth in SEQ ID NOS: 13, 14 and 15, encoding either of two LSDl polypeptides, which are preferably the LSDl polypeptides set forth in SEQ ID NOS: 16 and 17. This DNA molecule may be cDNA or genomic. The invention also includes as the open reading frame any chimeric construction comprising a promoter sequence and the DNA molecule of the invention, a recombinant plant transformed with the DNA molecule, and any transformation vector comprising the DNA of the invention. In addition, the DNA sequence of either the full-length SEQ ID NO: 13, or a shortened or otherwise modified version thereof, may be modified to optimize its expression in plants, with codons chosen for production of the same or a similar protein as encoded by the wild type LSDl gene. Other modifications of the LSDl gene that yield a protein having essentially the same properties as the LSDl gene are included within the invention herein. The invention herein also includes anything that hybridizes to the LSDl DNA (SEQ ID NO: 13) of the invention as discussed above, under hybridization conditions, which are defined as: 7% Na dodecyl sulfate (SDS), 0.5 M sodium phosphate, pH 7.0, 1 mM EDTA at 50C, and wash in 2X SSC buffer, 1% SDS, at 50C (Church and Gilbert, 1984). Proc. Natl. Acad. Sci. USA 81 :1991-1995 (1984)). The novel LSDl gene of the present invention, it its wild type form or as mutated by selected mutations and genetically engineered derivatives obtained as is known in the art, and proteins encoded thereby, are included in the invention herein, and may be transferred into any plant host using methodology known in the art for purposes of altering the extent and type of plant resistance to pathogens, and to change resistance to particular herbicides. The mutant phenotype of the null Isdl allele suggests that the wild type product is a negative regulator of cell death. In addition, Isdl reacts to both nominally virulent pathogens, and to chemicals which trigger the onset SAR, with an HR-like response. But it is important to note that Isdl expresses wild type timing of R gene driven HR (Dietrich et al, 1994)~it is the subsequent spread of cell death which distinguishes the mutant. Thus, cell autonomous signals required for R gene function are intact in an Isdl null, but the response to cell non-autonomous signals emanating from cells undergoing HR is perturbed. Collectively, these features of the mutant phenotype suggest that LSDl functions to limit both the initiation of defense responses and the subsequent extent of the HR. The fact that an Isdl null is hyper-responsive to signals initiating the defense response and HR-like cell death additionally suggests that these pathways are functionally intact in the wild type cell, but require a threshold level of signal for full activation. LSDl appears to act as a transcription factor (or as a protein which sequesters a transcription factor). As outlined above, the oxidative burst in an infected cell generates a superoxide-dependent signal up-regulating the HR pathway. This signal overcomes the negative regulatory function of the available LSDl, and drives primary responding cells into the HR pathway. Additionally, the cells undergoing HR amplify the signal, probably via a sustained extracellular oxidative burst, to neighboring cells. The primary signal molecule may be diffusible over short ranges (Levine et al., 1994), could act as an autocrine signal, and could lead to the accumulation of a secondary signal molecule in a steep spatial gradient from the infection site. At a critical point in the signal gradient, a threshold is reached. Above that point the pro-death pathway operates, and below it the pro-death response would be attenuated by LSDl. Such a gradient is formed by SA and SA-conjugates (Enyedi et al., 1992); SA biosynthesis can be induced by hydrogen peroxide (Leon et al., 1995); and sub- effective doses of SA can amplify pathogen-derived signals (Kauss et al., 1992; Kauss and Jeblick, 1995; Mauch-Mani and Slusarenko, 1996). Thus, it could be that an SA gradient dictates LSDl activity. Constitutive expression levels by LSDl could suffice to protect cells below the critical signal threshold for death induction. The time lag of 12-16 hours observed between superoxide production initiated in Isdl by a variety of triggers and the onset of cell death (Jabs et al., 1996), which could provide sufficient time for up-regulation of LSDl activity before irrevocable commitment to death during wild type responses, so that cell death could spread until sufficient active LSDl accumulates. Alternatively, this time lag could represent a requirement for biosynthesis of pro-death intermediates and LSDl normally could operate by interdicting this pathway. LSDl could positively regulate anti-cell death targets, potentially including genes involved in cell survival, ROI de-toxification, or in degradation of a key intermediate in the pro-death pathway. Alternatively, LSDl could act as a transcriptional repressor directly on genes in the pro-death effector pathway. This scenario differs from the first only in that the set of target genes would be different. The availability of extragenic suppressors of Isdl will aid in identifying LSDl targets (Jabs et al., 1996). This model also explains the runaway cell death phenotype of the null Isdl mutant. In the absence of LSDl, the threshold normally required before commitment to HR is removed. Thus, minimal up-regulation of the superoxide-dependent signal drives the cell into the HR pathway. Hence the ability of Isdl to respond to virulent pathogens as if resistant derives from a lack of background inhibition of the HR pathway normally operating in the cell. Moreover, extracellular superoxide produced during the oxidative burst initiates the same series of events in cells immediately surrounding the site of initiation, and the cell death propagation indicative of the Isdl phenotype results. Because the null Isdl mutant still requires superoxide for initiation of cell death propagation, it is unlikely that superoxide directly regulates LSDl activity. This further suggests that a superoxide-dependent signal is the autocrine which propagates the response to neighboring cells. The A. thaliana Isdl mutant phenotype is characterized by enhanced disease resistance, spontaneous formation of lesions in the absence of cell death initiators and failure to limit the extent of cell death. The wildtype LSDl protein therefore negatively regulates a cell death pathway involved in plant defense responses. The LSDl gene encodes a protein containing a novel zinc finger protein, which is included in the invention herein and is defined by its three consensus zinc fingers: CxxCRxxLMYxxGASxRxVxCxxC (SEQ ID NO:52). These three zinc finger domains have not been observed before in the range of zinc finger proteins. As shown in Dietrich et al., 1997, the LSDl gene is a key negative regulator of hypersensitive cell death in plants. We sought other versions of this consensus zinc finger sequence in other plant proteins. The data on homologies between the LSDl and LOLl and LOL2 zinc finger domains indicates that LSDl as well as LOLl and LOL2 are members of a novel subclass of zinc finger proteins that are involved in plant cell death pathways. LOLl and LOL2 might function in cell death phenomena leading to hypersensitive response and disease resistance as has been shown for LSDl . The homologues may also be involved in programmed cell death (PCD) pathways occurring in plants. Examples of PCD n plants include lateral root development, tracheary element differentiation, and abscission of leafs. Preliminary expression studies suggest that LOL2 is expressed in flowers and siliques. Thus a role for LOL2 in PCD pathways leading to petal senescence, anther dihiscence or PCD of nucellar cells is not unlikely. It is also possible that LOL2 is involved in the hypersensitive response and disease resistance in flowers, thus protecting seeds and ultimately the following generations from pathogen. Alternatively, LOL2 could be up- regulated during the hypersensitive response. Use of LOLl and LOLl should allow prediction of the protein's function with respect to protection from programmed cell death. The consensus sequences defined by the LSDl, LOLl and 1OL2 zinc finger domains (Figures 7-8) are thus far unique in the available deduced protein databases. Because zinc fmger domains of this type bind DNA and thereby regulate gene activation, it is highly likely that the consensus zinc finger domain defined here is required for proper regulation of related sets of genes. Furthermore, because zinc finger DNA binding domains of related sequence generally control related cellular processes, the new consensus defined here should also do so. Because LSDl is known to negatively regulate cell death induced by pathogens, it is highly likely that LOLl and LOL2 also control plant cell death. Thus, the utility of this portion of the invention lies in production of transgenic plants which have mutated versions of the LOLl or LOLl genes or which overexpress these proteins. Such plants will likely be more resistant to pathogen attack, if, in the first case, the LOL genes function to repress defense response (as does LSDl). Alternatively, if the LOL genes function to activate defense mechanisms, then overexpression will lead to a more effective pathogen response. Because zinc fmger proteins featuring other non-LSD 1 type DNA binding domains function to either activate or repress gene transcription, we cannot distinguish at present between these two models. The invention also includes plant proteins, and the genes which encode them, which directly interact with LSDl protein. Gene regulation in response to pathogen attack is controlled, in part, by the repression and activation of genes. The LSDl, LOLl and LOL2 proteins encode a novel branch of the zinc-finger DNA binding protein superfamily with roles in controlling plant cell death. As such, they are expected to interact with other proteins. Paradigms of gene activation currently demonstrate that DNA binding proteins can have two classes of "partners". The first class sequesters the DNA binding protein in the cell's cytosol. These partner proteins hold the DNA binding protein out of the nucleus until the correct cellular stimulus is received. This stimulus disrupts the physical interaction, and the DNA binding protein is free to migrate into the nucleus and activate or repress transcription. The second class of protein which interacts with DNA binding protein is made up of proteins which are partners having the role of "enhancing" the gene activation or repression encoded by the DNA binding protein. These partners are termed "co- activators" or "co-repressors" and they may or may not have intrinsic DNA binding activity. We have identified several genes whose protein products interact physically with the LSDl protein using a common assay, called a "yeast two-hybrid interaction trap" to detect such interactions genetically (Fields and Sternglanz, 1994; Finley and Brent, 1996). Because the inactivation of LSDl by mutation leads to enhanced disease resistance, the LSDl partner proteins represent novel targets for engineering plants with enhanced resistance to pathogens. Thus, this invention includes all proteins which interact with the cell death regulator LSDl (SEQ ID NOS: 66-91 (includes sequential pairs of nucleic acids and corresponding amino acid sequences). The features of the present invention will be more clearly understood by reference to the following examples, which are not to be construed as limiting the invention. EXAMPLES Example I Care and maintenance of plants Plants were grown in a chamber at 9 hours light per day, 22°C day temperature and 20°C night temperature essentially as described (Dietrich et al., 1994). Example II Isolation of DNA and RNA, probe preparation, cloning Small scale genomic DNA preps were made from single leaves (~lcm long rosette leaves) (Lukowitz et al., 1996). The DNA pellet was re-suspended in 50 ml of Tris/EDTA (TE) and 1 ml was used in a 20 ml polymerase chain reaction (PCR). Large scale genomic DNA preps were done based on the protocol of (Rogers and Bendich, 1985), modified such that concentration in the 2X hexadecyltrimethylammonium bromide (CTAB)(Sigma, St. Louis, MO) buffer was increased to 3% and the precipitated DNA was resuspended in Tris/EDTA/sodium chloride (TEN) buffer and digested with 100 mg/ml, followed by two extractions with chloroform/iso-amyl alcohol and a final precipitation. RNA was isolated by grinding fresh tissue in liquid nitrogen to a fine powder and extraction in 1 ml of Trizol reagent (Gibco-BRL, Gaithersburg, MD) per 100 mg tissue fresh weight. RNA was isolated according to the manufacturer's protocol. PolyA+ RNA was isolated using DynaBeads (Dynal, Oslo, Norway). RNA blots were formaldehyde agarose gels and contained either 15 mg total RNA or 1 mg polyA+ RNA. HyBond filters for DNA or RNA blots (Amersham, Little Chalfort, United Kingdom) were hybridized in 6xSSC, 5X Denhardt's solution, 0.1% SDS and 100 mg/ml sheared Herring sperm DNA at 65°C. Washes were in 0.2X SSC, 0.1 % SDS at the same temperature. RNA blots were stripped for re-hybridization in 5 mM TRIS/2mM EDTA, (pH8.0), 0.1X Denhardt's solution for 1 hour at 65°C. Example III Isolation of new CAPS markers and genetic mapping of Isdl After establishing linkage to the agamous {AG) co-dominant amplified polymorphic sequences (CAPS) marker (Konieczny and Ausubel, 1993), we subcloned and end- sequenced a 1.6 kb Hindlll fragment from the RFLP cosmid marker g3883 (position 73.5 on the Arabidopsis RI map; Lister and Dean, 1993; see http://nasc.nott.ac.uk/RI_data/top_frame.html), and primers designed based on this sequence. This primer set amplified a rapid amplified polymorphic DNA (RAPD) marker (size difference in Ws-0 versus Col-0 without restriction digestion), and map data generated using this primer allowed us to place Isdl below (telomeric to) it. Probe B9-1.8, isolated as a 1.8 kb Sstl-EcoRI fragment from the JGB9 genomic phage clone (RI map position -75; gift of Dr. George Coupland, Cambridge Laboratories, Norwich U.K.) was converted into a CAPS marker. Mapping of this polymorphism placed Isdl above (centromeric to) it (Fig. 2). Recombinants were identified as homozygous for one of these CAPS markers, and heterozygous for the other using DNA from F2 individuals. F3 progeny from these recombinants were then scored as either homozygous Isdl, segregating Isdl, or homozygous wild-type for lesion spread. All CAPS markers we developed are described in Table 1 (below). Table 1. New PCR based RFLP (CAPS markers derived during cloning of Isdl Marker Enzyme PCR prod. Col-0 Ws-0 ch42 Clal 1.4 kb 750 bp 1.4 kb 650 g3883-1.6 none 1.4 kb 0.7 kb (uncut) (uncut) gl3838-1.4 Hinfl 1.4 kb 450 bp 450 bp 330 330 280 280 200 160 B9-1.8 Hinfl 1.8 kb 420 bp 420 bp 260 260 240 180 180 160 140 140 1H1L-1.6 Ddel 1.6 kb 1.0 kb 700 bp 300 bp 300 (doublet?) 5F7R-1.5 NlalV 1.5 kb 1.0 kb 1.2 kb 250 bp 250 bp 200 bp 0B4-1.6 Ddel 1.6 kb 900 bp 700 bp 400 400 220 180 180 8A6-1.3 Taql 1.3 kb 800 bp 800 bp 400 250 220 150 Example IV Map refinement YACs were defined (Schmidt et al., 1995; Schmidt et al, 1996, http://genom.e- www.stanford.edu/Arabidopsis/JIC-contigs.html), confirmed by DNA blotting to establish a contig and their ends were isolated by vectorette PCR as described (Matallana et al., 1992; Grant et al., 1995). These ends were also used to isolate genomic phage from a Ws-0 genomic library (Fig. 1). Insert fragments of 1-3 kb were cloned into PBS and end sequenced for derivation of primers identifying new CAPS. PCR conditions (DNA Engine MJ Research) for all CAPS primer pairs except 8A6-1.3 and Isdl deletion primers are: 92°C, 3'; 35 cycles of (denature 92°C, 30"; anneal 50°C, 30"; extend 72°C, 2'30"); 72°C, 3'. For 8A6-1.3 and the Isdl deletion primer pairs we used 53°C annealing. Table 2 shows the primer sequences used to identify new CAPS markers. Table 2. Primer sequences used to identify new CAPS markers used for cloning Isdl ch42 for 5'-cag tgg ate ttt cct cag acg-3' (SEQ ID NO: 18) ch42 rev 5 '-cat ctt ctt ctg caa tct ggg-3' (SEQ ID NO: 19) g3883-1.6 for 5'-cat cca tea aac aaa etc c-3' (SEQ ID NO:20) g3883-1.6 rev 5'-tgt ttc aga gta gcc aat tc-3' (SEQ ID NO:21) gl3138-1.4 for 5'-cac gtt agt tag tta gaa gg-3' (SEQ ID NO:22) gl3138-1.4 rev 5'-ctg atg ttc tct aca aat gg-3' (SEQ ID NO:23) B9-1.8 for 5'-cgt ate cgc att tct tea ctg c-3 ' (SEQ ID NO:24) B9-1.8 rev 5'-cat ctg caa cat ctt ccc cag-3' (SEQ ID NO:25) 1H1L-1.6 for 5'-ttg agt cct tct tgt ctg-3' (SEQ ID NO:26) 1H1L-1.6 rev 5 '-eta gag ctt gaa agt tga tg-3' (SEQ ID NO:27) F7R-1.5 for 5'-gaa tgg tgt aac caa act c-3' (SEQ ID NO:28) F7R-1.5 rev 5 '-cat ace gta tga tgg aac-3' (SEQ ID NO:29) 0B4L-1.6 for 5'-gaa etc art gta tgg acc-3' (SEQ ID NO:30) 0B4L-1.6 rev 5 '-eta aga tgg gaa tgt tgg-3' (SEQ ID NO:31) 8A6-1.3 for 5'-cca aga aga gaa aac gga ga-3' (SEQ ID NO:32) 8A6-1.3 rev 5'-aac aat agg agg tgc aga gt-3' (SEQ ID NO:33) Primers to amplify across the Isdl deletion: Isdl far side: 5'-acc taa caa aaa gaa aag tgt gtg agg-3' (SEQ ID NO:34) Isdl outside 5'-ata ata aac cct act age tct aac aag-3' (SEQ ID NO:35) Isdl alt. spl. 5' 5'-ctg eta ctt tea tec aaa c-3' (SEQ ID NO:36) Example V Vector construction for complementation The Agrobacterium vacuum infiltration procedure was used to generate transgenic plants (Bechtold et al., 1993; Grant et al., 1995). Vectors were derived from pGPTV-Hyg (Becker et al., 1992) as follows: pSGCGF was made by restricting pGPTV-Hyg with Hindlll and Sad and replacing this fragment with a Hindlll-Sacl fragment containing the polylinker from pIC20H (GenBank accession L08912; provided by Steve Goff, Novartis, Research Triangle Park, N.C). Either the 7kb Xhol or 4.5 kb Pstl-Xhol genomic fragments were cloned into this, the former into the unique vector Sail site, the latter as a Sacl-Sall fragment derived from an intermediate cloning step into pBS as a Pstl-Xhol fragment. The pHyg35S vector was made by cloning a four enhancer-containing 35S promoter fragment as a Hindlll-Xbal fragment into pGPTV-Hyg (provided by Dr. Douglas C. Boyes, Univ. of North Carolina, Chapel Hill). The EST 82D11 cDNA sequence was isolated as a Sall-Xbal fragment from pZLl (Newman et al., 1994) and cloned into Xhol-Xbal digested pHyg35S. Example VI Cloning The genomic Ws-0 library in 1GEM11 was a gift of Dr. Kenneth A. Feldmann (Univ. of Arizona). The cDNA library is an oligo-dT primed library prepared from polyA+ Col-0 mRNA from leaves cloned into IZAPII (Stratagene, La Jolla, CA) according to the manufacturer's instructions (gift of Dr. Douglas C. Boyes and Dr. Murray R. Grant). Example VII LSDl sequences The sequences of the LSDl cDNA (SEQ ID NOS: 14 and 15) and the 4.5 kb LSDl Xhol-Pstl genomic fragment (SEQ ID NO:13; the longest 5'LSDl cDNA starts at base 1892 of this sequence) are deposited in GenBank as accessions U 87833 and U 87834, respectively. Endpoints of the various LSDl cDNAs isolated are shown in Table3A and examples are provided by SEQ ID NO: 14 (short form from cDNA MG7 as shown in Table 3) and SEQ ID NO: 15 (long form, from cDNA MG8). The polypeptides deduced from these are shown in Fig. 11-12, respectively. Table 3B shows the sizes of each intron deduced from comparison of the sequence shown in SEQ ID NO: 13. Table 3. Sequence characteristics of the LSDl gene Endpoints of independent LSDl cDNAs cDNA 5' end point Alternate splice 3' end point MG7(2) C l short A 1021 EST 82D1 1 A 27 short T 1031 MG4 C59 short A 1188* MG10 C 59 short G 1225 MG5 G 67 short A 1205 MG2 (4) G 90 short A 1106 MG8 (2) G 98 long A 1082 MG16 (2) C 103 short A 1066 MG11 C 117 long G 1225 Numbers in parentheses refer to the number of isolates of the same clone. Nucleotide numbers at the 5' and 3' ends refer to nucleotide positions from SEQ ID NO: 13. An A at the 3' endpoint can be either an A in the genomic sequence or the first A of the polyA tail. The endpoint marked with an * had no polyA tail. Intron sizes intron # size in nucleotides 1 88 2 (short splice) 68 2 (long splice) 129 3 89 4 489 5 100 6 92 7 87 Intron splice junction positions are located at bses 198-199, 260-261, 447-448, 552-553, 692-693, 764-765, and 836-837 in SEQ ID NO: 13. Example VIII Genetic and physical mapping of Isdl The Isdl mutation segregates as a monogenic recessive (Dietrich et al., 1994). F2 progeny of a cross between Isdl (Ws-0 background) and Col-0 (LSDl) were analyzed using the co-dominant amplified polymorphic sequences (CAPS) mapping procedure (Konieczny and Ausubel, 1993) to first establish linkage to the AG marker on chromosome 4. The closely linked gl3838 probe (3 recombinants in 1632 meioses) was used to identify YAC (yeast artificial chromosome) clones (Schmidt et al., 1995; Schmidt et al., 1996). We constructed a physical contig of these YACs, shown in figure 1A. We used labeled YAC ends CIC1H1L, yUP5F7R and EG20B4L to isolate genomic phage clones, subcloned fragments form each of these, end-sequenced the subclones, derived primer sequences and developed new CAPS markers (see Tables 1 and 2). The CAPS markers 1H1L-1.6 and 5F7R-1.5 mapped closest to Isdl (1 and 3 recombinants, respectively from 2054 meioses); see Tables 1 and 2 for new CAPS markers). We hybridized these two CAPS markers to filters containing bacterial artificial chromosome (BAC) clone arrays (Choi et al, 1995, distributed by the Arabidopsis Biological Resource Center, Ohio St. Univ.), and isolated the five BAC clones depicted in Figure 2B. Because 5F7R-1.5 and 1H1L-1.6 genetically flank Isdl (Figure IB), BAC clone 1G5 should contain the gene. As 1 G5 was the only BAC clone to physically span the relevant genetic region, we connected BACs 6H3 and 8A6 by walking in a genomic phage library. We defined a 5kb Hindlll fragment from BAC 8A6 which hybridized only to itself and BAC 1G5. When used as a probe on filters containing restriction digests of the relevant BAC clones, this fragment hybridized to a 1.3 kb EcoRI fragment which also was present only on BACs 8A6 and 1G5. This 8A6-1.3 clone, (small box in Figure 1C) was used to isolate three phage clones, two of which are depicted in Figure 1C. Labeled inserts from each detected BAC clones 1G5, 6H3 and 8A6, thus providing multiple redundancy of genomic cloned DNA encompassing Isdl. We also converted 8A6-1.3 into a CAPs marker, and found that it co- segregated with Isdl in 2054 meioses. This map resolution of approximately 0.05 map units, suggested that Isdl was within 5-15 kb (at 100-300 kb per map unit; Schmidt et al., 1995; Schmidt et al., 1996) in either direction of 8A6-1.3. We probed genomic Arabidopsis DNA blots of digested wild type Ws-0 and Isdl to confirm co-linearity of the cloned and genomic DNA immediately surrounding 8A6-1.3. We noted that a variety of fragments detected a genomic DNA rearrangement in Isdl relative to wild type Ws-0 (data not shown). This rearrangement corresponded to a loss of restriction sites and a deletion as noted in Figures 1C and 3C. The Isdl mutant comes from an Agrobacterium mutagenized population of Arabidopsis, and it is known that the transformation procedure can generate non-T-DNA associated mutations (Feldmann, 1991). We subcloned and sequenced various wild type genomic DNA fragments at this position, and compared their sequences to several databases, including the Arabidopsis EST database (Rounsley et al., 1996, http://www.tigr.org/tdb/at/at.html). One EST clone (EST 82D11T7; GenBank accession T45220) exhibited blocks of identity to our genomic DNA sequence, suggesting the presence of introns in the latter. Because the gene encoding this EST is largely deleted in Isdl, it became a candidate LSDl gene. Example IX Complementation of Isdl To confirm that the genomic deletion encompasses LSDl, we constructed subclones from the genomic phage as shown in Figure 3C for complementation into the T-DNA binary vector pSGCGF. Because the typical method for generation of transgenic Arabidopsis, vacuum infiltration of Agrobacterium carrying binary T-DNA vectors, triggers the propagative cell death indicative of the Isdl phenotype, we devised an alternate complementation strategy. We transformed FI plants of Isdl x Col-0, and plated surface- sterilized seeds of the next (F2) generation onto media containing hygromycin as a selective antibiotic. We then identified hygromycin resistant transformants which were homozygous for Ws-0 alleles at 5F7R-1.5, 1H1L-1.6, and 8A6-1.3, and thus were Isdl/lsdl homozygous mutants. These individuals contained both mutant and wild type alleles for the CAPS marker which spans the Isdl deletion, because a wild type allele is present on the transgene. These transgenic plants were treated with droplets of 2,6-dichloroisonicotinic acid (IN A); 0.3 mg/ml wettable powder containing 25% active ingredient, Uknes et al., 1993a) a potent inducer of SAR and the Isdl phenotype (Dietrich et al., 1994). If the mutation were complemented, then INA treatment should not lead to spreading cell death. Table 4 shows that transgenic plants carrying either the 7kb Xhol fragment or the 4.5 kb Pstl-Xhol (Figure 3C) all survived this treatment, and are thus complemented for the Isdl mutation. Selfed F3 progeny from a complemented F2 individual carrying either the 4.5 kb Xhol-Pstl fragment or the 7 kb Xhol fragment were also analyzed. All F3 progeny which inherited the transgene were complemented (Table 4), while all of their non-transgenic sibs still exhibited the Isdl phenotype (data not shown). In no case did wild type control plants exhibit spreading cell death after INA application. Table 4. Complementation of the Isdl mutant # of plants complemented/# transgenics tested from: Construct Independent F2s Transgenic F3 progeny 7 kb Xhol 1/1 A 20/20 B 3/3° 21/21° kb Pstl-Xhol 2/2 A 14/14 B 35S-cDNA 1/1 Λ 19/19 B ■ x Selected for hygromycin resistance and screened for homozygous Ws-0 alleles through the Isdl genetic interval as described, except where noted in . Individual F s were both drop tested with INA and shifted to LD conditions (Dietrich et al., 1994). B Selfed progeny from a complemented F individual (homozygous Ws-0 alleles through the Isdl interval) were screened by PCR at F for presence of the hygromycin resistance gene and then INA tested, c F parents were identified as hygromycin resistant and heterozygous through the Isdl interval, then selfed and re-screened as hygromycin resistant and homozygous Ws-0 through the Isdl interval at F before INA testing. Due to low numbers of independent F2 transformants which were homozygous mutant through the Isdl interval from the original transformation, we also isolated F2 transformants carrying the 7 kb Xhol fragment which were originally identified as heterozygote at the CAPS markers flanking Isdl. Selfed progeny from these should segregate both the transgene and the Isdl mutation. Among these progeny, we identified F3 individuals which were homozygous Ws-0 through the Isdl interval and carried the transgene. As shown in Table 4, these also were all complemented for protection against INA-induced spreading cell death. We conclude that the 4.5kb Pstl-Xhol fragment carries the Isdl gene and sufficient cis control elements to ensure its expression. All transgenic plants complemented for the INA-induced Isdl mutant phenotype were also complemented for initiation of spreading cell death after transfer to non- permissive long day conditions as well (Dietrich et al., 1994; not shown). Thus, the complementing DNA corrects the mutant phenotype induced by two independent stimuli. Example X Identification of alternately spliced LSDl transcripts We sequenced all of the complementing 4.5 kb Pstl-Xhol genomic DNA fragment (SEQ ID NO: 13), eight independent cDNAs (Example VII) and completed the sequence of the full 82D11T7 EST sequence. Among the cDNAs, we identified two classes expressing open reading frames of either 184 or 189 amino acids (SEQ ID NO: 16 and 17). An alternate splice which adds 61bp to the 5' region of some cDNAs also provides an alternate translation start, hence, the extra five amino acids in SEQ ID NO: 17. The sequences of both cDNA classes matched exactly the genomic sequence except at the positions of 7 introns (see Table 3). Nucleotide 1 of the longest cDNA is at position 1892 in the 4.5 kb Pstl-Xhol genomic sequence (SEQ ID NO: 13 ). Thus, 1891 nucleotides of promoter are sufficient for appropriate expression in complementation of the Isdl mutation. The cDNA 5' ends are clustered (Table 3), suggesting that the longest could be full length. We also complemented the Isdl mutation by transformation of the full insert from EST clone 82D11T7 expressed from the strong and constitutive cauliflower mosaic virus 35S promoter (see Table 3) proving that this cDNA contains the entire LSDl coding region. The 3' ends of these cDNAs are very heterogeneous, suggesting the presence of multiple polyadenylation addition signals (Table 3). No other significant open reading frames were observed in the 4.5 kb Pstl-Xhol genomic clone. When either the EST 82D11T7 clone, or a 0.8 kb EcoRI-Xbal genomic fragment covering the Isdl deletion were used as probes on RNA blots, a rare mRNA of approximately 1.2 kb was detected in leaf tissue of wild type Ws-0 plants (Figure 3). This length is consistent with the size of the longest cDNA, supporting the conclusion that we have identified a nearly full-length transcript. Importantly, this mRNA was completely lacking in mRNA prepared from Isdl leaves, furthering the argument that it encodes LSDl . The finding that Isdl is an mRNA allele was corroborated by sequencing across the genomic deletion in the mutant (Figure 3). The 5' border of the deletion is an A at nucleotide 55 and the 3' boundary is in the fourth intron (data not shown). It is noteworthy that expression of this candidate mRNA was unaffected by application of INA (Figure 4, top). The expected high level of INA-induced PR-1 mRNA accumulation in leaves of both wild type and Isdl (Figure 4, middle) served as a control in this experiment for efficacy of INA treatment. The Isdl phenotype can be observed in all cell types examined after initiation of lesion formation (Dietrich et al., 1994). RNA blot analysis of seedlings, stems, leaves and flowers demonstrated that the LSDl gene is expressed constitutively in each of these Arabidopsis tissues (data not shown). Thus, the requirement for LSDl activity in these tissues is consistent with the gene's expression pattern. Example XI The LSDl mRNA encodes a novel zinc-finger domain We searched a variety of databases with the predicted translation product of the LSDl cDNA sequence. Several striking features emerged. First, there are three zinc-finger domains, depicted in Figure 5 (SEQ ID NOS: 1-3), which share remarkable homology with one another. These are C-x-x-C, or type IV, zinc-fingers, according to the classification of Sanchez-Garia and Rabbitts (1994), and they share most homology with plant relatives of the GATA-1 transcription factor (Evans and Felsenfeld, 1989; Omichinski et al., 1993). The plant members of this sub-family described to date include the CO gene, which controls transition to flowering (Putterill et al., 1995), a set of related DNA binding proteins (Yanagisawa, 1995; De Paolis et al., 1996) and a gene whose transcription is salt stress- induced (Lippuner et al., 1996). None of these proteins shares with LSDl the consensus homology within the Zn-fingers. The second homology domain is derived from the carboxy 1 portion of LSDl, from residues 129 to 180 (Figure 6-SEQ ID NO:4). This region of LSDl exhibits homology to three broad classes of regulatory proteins. First, all mammalian insulin receptor substrates; second, a set of animal transcription factors; and third, a maize transcription initiator binding protein. The conceptual LSDl translation product also identified two additional Arabidopsis ESTs via their predicted amino acid homology. Importantly, each has at least one C-x-x-C Zn-fmger and most of the associated consensus residues found in the LSDl internal homologies. They are ESTs 172A7T7 (GenBank R6552)(SEQ ID NO: 58 and 132J21T7 (GenBank T45809). Thus, it is probable that LSDl is the first member of a widely distributed Zn-fmger sub-family in plants, defined by the internal homology within each zinc-finger. The other amino acids in the consensus section are not known to be found in any other zinc finger proteins. Example XII Identification of expressed target sequence tags (EST) and cDNAs containing LSDl -type zinc finger domains As discussed in the text prior to the Examples, the predicted amino acid sequence of the LSDl zinc fingers was used to search the GenBank database (NCBI). Two Arabidopsis thaliana ESTs (EST132J21T7 and EST 172A7T7) were identified, each of which contains at least two zinc finger domains and most of the associated consensus residues found in the LSDl internal homologies (Dietrich, 1997). These ESTs were ordered from Ohio State University Arabidopsis Biological Resource Stock Center and resequenced. Sequences were analyzed with the Genetics Computer Group programs (Devereaux et al.,1994). A specific probe isolated from EST172A7T7 was subsequently used for screening of cDNA and genomic libraries. The bacterial strain carrying EST132J21T7, however, was not viable. Therefore, degenerated primers were designed based on the EST132J21T7 sequence. Genomic Arabidopsis thaliana Ws-0 DNA was used in the PCR reaction and gave rise to a specific PCR product of approximately 400 bp. This fragment was subcloned via the TA Cloning Kit (Invitrogen, Carlsbad, CA) into pBluescript KS(+). Two new genes were identified as described here. Their predicted protein products are highly related to that of LSDl indicating an involvement in the control of cell death in plants Example XIII LOLl cDNA Poly A + RNA isolated from uninduced and P. syringae DC3000 induced Arabidopsis thaliana Col-0 leaf tissue was reverse transcribed. The resulting cDNA population was subcloned unidirectionally into the EcoRI/Xhol - sites of a lambda-Zap II vector using the cDNA-synthesis Kit (Stratagene, La Jolla, CA) according to the 6 manufacturer's directions. The titer of this MG-library was calculated as 2.5 x 10 pfu 5 Approximately 8x10 pfu of the amplified MG-library were subsequently screened with α P dCTP labeled probes (Stratagene 'Prime it' Kit) specific for EST132J21T7 or EST172A7T7. With the probe specific for EST132J21T7, four cDNA clones were identified and subcloned via the Stratagene excision system. One clone contained an insert of less than 100 bp in length and was not further analyzed. The three remaining clones were sequenced by standard protocol (primers: M13F, M13R, PE6, and PE7); for primer sequences refer to Table 5, below). Clones 2 and 3 contained identical open reading frames (ORFs) and were homologous to EST132J21T7 and to another identical and overlapping EST clone, EST119C9T7. The fourth clone consisted of a chimeric cDNA of approximately 1500 bp, with approximately 400 bp similarity to EST132J21T7, EST119C9T7, and clones 2 and 3. It was also not analyzed further. Table 5. Primers and primer sequences used Primer Primer Sequence SEQ ID NO: M13F 5'-GTAAAACGACGGCCATG-3' 37 M13R 5'-GGAAACAGCTATGACCATG-3' 38 PE6 5'-TTCATGGCAATGGTGTGACCCC-3' 39 PE7 5 ' - CTG CCG GAT TCT TGA TCG A AG A -3 ' 40 PE8 5'-AGAGGAAGGTCCGCCTCCGG-3' 41 PE9 5'-CTCTGCTCTCCTGAGACTGCTT-3' 42 PE13 5'-CATCATAATGTCTCCTTTTGAGAC-3' 43 PE15 5'-GCCATCCATTATTCATCGCCT-3' 44 PE23 5'- GAG GAG GAA GAA CTG CAG ATT CC -3' 45 PE30 5'- GTG CTC CAT GTC CAA ATC ATA C -3 ' 46 Clone 2, with an insert length of 908 bp represents a full length cDNA clone, as determined by the presence of an open reading frame flanked by untranslated sequences, and was renamed LOLl (Z,sd one Λke)(SEQ ID NO:47). We confirmed that the LOLl cDNA and EST132J21T7 are encoded by the same gene using genomic DNA (Southern) blot analysis (data not shown). The LOLl protein of 154 amino acids (SEQ ID NO:48) contains three zinc fmger domains of the LSDl -type (SEQ ID NOS:49-51). The consensus sequence of the LOLl zinc finger domains is defined by CxxCxxLLMYxxGAxSxCxxC (SEQ ID NO:53). Example XIV LOL2 cDNA By screening the MG-cDNA-library, no clones homologous to EST172A7T7 could be obtained. Therefore, the AB-cDNA-library (derived from RNA isolated from different tissues of sterile grown plants, available at the European .Arabidopsis Stock Center, 32 Cologne, Germany) was screened with α P dCTP labeled probe specific for EST172A7T7. Six homologous cDNA clones were obtained and subcloned into the Smal site of pBluescript KS(+). Restriction analysis indicated that the inserts were encoded by the same gene. Only the longest insert was sequenced following standard protocol (primers used: M13F, M13R, PE8 and PE9: for primer sequences, refer to Table 5. We demonstrated that this insert contained an ORF of 500 bp homologous to EST172A7T7. This non-full length cDNA was designated LOLl (SEQ ID NO:54). The deduced protein (SEQ ID NO:55) consisting of two LSDl -type zinc fmger domains extending from bases 130-195 and 244- 309 of SEQ ID NO:54 (SEQ ID NOS:56-57, respectively). Comparison to EST172A7T7 shows that the EST (SEQ ID NO:58) contains a 124 bp insertion (bases 386-509 after the second zinc finger of SEQ ID NO:58), leading to a different C-terminal. Comparison of these two partial cDNA sequences with the genomic LOLl sequence (see below) demonstrates that they are alternate splice forms from the same gene encoding two related proteins. This conclusion is strengthened by the fact that the LOLl cDNA and EST172A7T7 hybridize to the same genomic DNA fragment and therefore are encoded by the same gene (data not shown). Thus, sequence analysis of genomic LOLl clones shows that the non-identical C-termini of LOL2 and EST172A7T7 are due to alternative splice sites. The genomic sequence of LOLl (SEQ ID NO:59, has a putative TATA-box sequence and polyadenylation signal (bases 922-930 and 2539-2544), and the exon borders of an alternative splice site (bases 2256-2382). The derived amino acid sequence extends from bases 1231-2462. Example XV Isolation of genomic LOL2 sequences from an Arabidopsis thaliana Col-0 library 5 8 x 10 genomic lambda clones (lambda GEM11, European Arabidopsis Stock 32 Center) were screen with a α P dCTP labeled probe specific for EST172A7T7. Nine clones homologous to LOLl EST172A7T7 could be identified. Restriction analysis demonstrated that the nine clones belonged to five different classes. Inserts ranging from two to five kb in size were isolated and subcloned into either Sad ore BamHI sites of pBluescript KS(+). Sequence information derives from two overlapping clones, sequentially sequenced with primers M13R, PE9, PE13, PE15, PE23 and PE30 (see Table 5). The genomic LOL2 sequence has a length of 3060 bp. Promoter and 5' untranslated regions consist of approximately 1200 bp. The translation products are encoded by three exons, which are interrupted by two introns of 182 bp and 458 bp length, respectively. The overall length of the coding sequence is 1232 bp. Due to alternative splice sites, two proteins which differ in their C-terminal regions are encoded by the LOLl gene (SEQ ID NO:59). A first protein, of 155 amino acids (SEQ ID NO:60), is identical to the LOLl cDNA and contains two zinc finger domains of the LSDl -type. The other translation product corresponds to EST172A7T7, consists of 147 amino acids, and contains two and a half zinc finger domains (SEQ ID NO:61). The consensus sequence of the two zinc finger domains of LOL2 is CxxCxxLLxYxxGxxxVxCSSC (SEQ ID NO:62). Example XVI Obtaining interacting genes The methodology for this Example is known to those skilled in the art and summarized in Fields and Sternglanz, 1994, and Finley and Brent, 1996. The LSDl short or LDS1 long open reading frames were cloned into the "bait vector" pEG202 of the TM commonly available LexA yeast two-hybrid system (Matchmaker , Clonetech, Palo Alto, CA) to generate plasmids pEG202-L and pEG202-S. These encode fusion proteins of the LexA DNA binding domain and the full length LSDl protein of both long and short isoforms (SEQ ID NOS 14 and 15). Yeast strain EGY48 is transformed with this plasmid, and appropriate controls performed to ascertain the LSDl fusion protein encoded by plasmids pEG202-L and pEG202-S did not intrinsically activate expression of the yeast markers used in this system. A yeast gene expression library was constructed in plasmid pJG4-5 using RNA from Arabidopsis leaves infected with Pseudomonas syringae. This library encodes fusion proteins of expressed Arabidopsis genes and the B42 transcriptional activation domain. The library was transformed en masse into the yeast strain EGY48 carrying either plasmid pEG202-L or -S. From an equivalent of 6 million clones screened, 122 were isolated. The longest insert of a member from each of these classes was sequenced using standard DNA sequencing methods. Because the novel Arabidopsis gene so identified is produced as an active translation fusion in this system, one is immediately able to identify the deduced protein sequence. The most interesting sequences thus defined, and their deduced protein sequences, are set forth herein as SEQ ID NOS: 66-91. The first main class of LSDl -interacting proteins has no database homologues. These proteins encode putative "sequestration" proteins for LSDl whose function is to inhibit LSDl function until the correct pathogen signal is received. Their utility lies in manipulation of the interaction with LSDl in plant cells such that LSDl is altered in its ability to regulate the response to pathogen. Alternatively, these novel LSDl -interacting proteins may encode new components of the gene regulation machinery working together with LSDl to control transcription in response to pathogen infection. These proteins are valuable because of the knowledge that LSDl is a key regulator of cell death in plants in response to pathogens. Proteins which physically interact with LSDl share in this cellular function. The second class defines proteins having database homologies to other proteins, strongly suggesting a role in control of gene transcription (e.g., CAAT box binding proteins which are known to bind the common CAAT regulatory unit in DNA preceding nearly all genes encoding eukaryotic mRNA). This finding is completely consistent with the embodiment described above, in which the LSDl partner proteins identify other components of the gene regulatory machinery required for response to pathogens. Manipulation of the expression of, for example, CAAT box binding proteins, will result in altered response to pathogen infection. While the invention has been described with reference to specific embodiments, it will be appreciated that numerous variations, modifications, and embodiments are possible, and accordingly , all such variations, modifications, and embodiments are to be regarded as being within the spirit and scope of the invention. LITERATURE CITED Baker, C. J. and Orlandi, E. W. (1995). Active oxygen in plant pathogenesis. Annu. Rev. Phytopathol. 33, 299-322. Bechtold, N., Ellis, J. and Pelletier, G. (1993). In planta agrobacterium-mediated gene transfer by infiltration of Arabidopsis thaliana plants. C. R. Acad. Sci., Paris 316, 1194- 1199. Becker, D., Kemper, E., Schell, J. and Masterson, R. (1992). New plant binary vectors with selectable markers located proximal to the left T-DNA border. Plant Mol. Biol. 10, 1 195- 1197. Bent, A. (1996). 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Acids Res. 13, 3403-3410. 1 SEQUENCE LISTING SEQ ID NO: 1 LVCHGCRNLLMYPRGASNVRCALCNTI MV SEQ ID NO:2 11CGGCRTMLMYTRGASSVRCSCCQTTN V SEQ ID NO:3 INCGHCRTTLMYPYGASSVKCAVCQFVTNV SEQ ID NO:4 MSNGRV- PLPTNRP-NGTACPPST- STSTPPSQTQTVWENPMSVDESGKLVSNV SEQ ID NO:5 MSPG-VAPVPSNRKGNGDYMPMSPKS S P-QQIINPIRRHPQRVDPNGYMM SEQ ID NO:6 VPLPTNRP-NGTACPPSTSTSTPPSQTQTVWENPMSVDESGKLVSNV SEQ ID NO:7 VPLPANNPW-TTWPSTPPSQPPAVCPPW SEQ ID NO:8 VPLPANNPW-TTVVPSTPPSQPPAVCPPVV SEQ ID NO:9 IPVYTNSNV-GTALPPSVSPSVSPSVT SEQ ID NOrlO WLP-NAAPAGAAAPPSGSRSTSPS SEQ ID NO: 11 SNGRVPLPTNRPN-GTACPPSTSTSTPPSQTQTVWENPMSVDESGKLVSNV SEQ ID NO: 12 SRA VPVPAADPNAG-AIVPANKSKRSPEQGQRRIRR SEQ ID NO:13 10 30 50 GATCAAATCTAGTTACGCTTAAATTTGGATATATCTAAGGTTTCTTCGTCAATATATGGA 70 90 110 GCTTACGAAAACGAAAGAGTGAGCTACGAGGAACTAAATCAATGAAGATAAGAGGAATGA 130 150 170 AGGAGAGAAGATCACCAAGGTGTAGAAATTTCTGAAGTCGTCTCCTCCAATCTCCACTAT 190 210 230 TGGTTTGTTCAGAACTTGAGAAGGCCTTAGATCCAAGCCATTAGTAACCTCTCTATGGCC 250 270 290 ATAAGTGACCTTAAGAGAGACCAACCTCGTGAAAGGATCAAGAACATCTCCAACAACACT 310 330 350 GCCGACCACGAGAGGATCTCTACGACTTAAAGACATATTTATCTTGGATCTCAAGTATCT 370 390 410 CAATAAAATGTTTTGCTTCTAACCTTATGAACCCTTACTTGCTATTCTTTATATAACGTT 430 450 470 TTGGGAATTGCAATAATTAGCTATTTAGCTTTATTCTCTCCAATGAAATCATTACCAGGG 490 510 530 TCTTTTCGTGTATAGTTATCTTCGAGAATCTACAACTCGTTCAACGTACGTATATCACTT 550 570 590 ATAATTCATGTTTTTTTTTCTTTCCTTTTTTCTAAATTTATAGTATTCTTATTCCAAAAC 610 630 650 CCACCAGTATAAAACAGAAATAATCATATTCCAAATTATACATCATCCACTTGTTTCTTG 670 690 710 CTAGCCACTAGTATGTAATTTATTCTGACTTATCATTGGAACTTCATGAACTATTTAAAA 730 750 770 TAATGTCACAAGCATATAATATGCTGCATATTTGCGTACGTCACGCATTTTGCGTCACAT 790 810 830 GTCACTCATTTAAATAGTTAAGGACACTACATTACACCGATTATGTATGATGTTAATGCA 850 870 890 TTTTAGAATAACTCCTTCAACCTAAACCATCATATAAAAGTATATATGCTCCAGATAAAT 910 930 950 TGACGCCATAATTGTTCACATATCTGGTTGGTTTGTACATACGTACTAGACTCTTTTTTT 970 990 1010 TCTTTTCTTAATGTAGTACTAAACTTAATTAATACCATCAAAAATATCAATTTAACAAAA 1030 1050 1070 CAAACCAGTAAAACTTTTAAAACAATGGAGTAAATCAAATAAAACAAGTAAATTAACAAA 1090 1110 1130 TAGACACAAGGTAACAGAAGTATAATAACGACAGAAAAATGAACAATTGGCCAAAAAATT 1150 1170 1190 CGTTTTCAAACGTGATTTCAAAATTGTCTCCAAATCTTAAATGTTGATAAAGTAATTTTT 1210 1230 1250 TTTTAAATTCATTATACCTTTCAAAAACAAGTGTATTACCTAAAAGCTCAACCGTGTATT 1270 1290 1310 CTTACACTCCAAACAAATTTAGTTCCCCAAGTTTGGAAGACAAAAATTTCTAAGAAATTT 1330 1350 1370 CTGACAAAACACATGAGAAATAAACCGATAAAGACTTCTAAAAACTATTGCAGACCAGTT 1390 1410 1430 TCATTTGCTGACCACAAAAAGTCATGAGAATACAATTAGCTCAGTGATTCTTGATATTTC 1450 1470 1490 TGGTACCTAACAAAAAGAAAAGTGTGTGAGGTTAGATGGCTATGATTTTTGCTCTCCAAT 1510 1530 1550 TTATTGTCCATTTCCCCAATTTGTAATATGAAATGCGCAAATTACTCTTCTTCCGATATG 1570 1590 1610 AATAAGCAAACGAAAACATACGTGGGACGTTATGTTGAGAACATTTGATTAAAGTTTATA 1630 1650 1670 TGCGATTTTCATTTATTTACTATGAATTTTTTGTTTGGCAGCATGTACGATTTTTCATTT 1690 1710 1730 AACACACAAATATTATAGAATTTTCATTGGTTCAAAGGGGTAGACAAAAAATAATTTAAT 1750 1770 1790 ATTATTACACCATTTGCAGAAAATTAGAAAATATATTTTTACCCATAATTAATTGATCTA 1810 1830 1850 TGGACGTATGCTTGGCATAAAAATTCATATTTAATTAGCAGAAGCCAATCGCTGCGTTTG 1870 1890 1910 TATATACGCGTTTATGACCGAGAAAAAAACCCTTACGCGTCATGTAAAAAAAAAAGAAGC 1930 1950 1970 GTAAATTACGAAAAACAGAGAGATAAATCCGGGCATTGAGATTTTGGAGATAGAGAGAGA 1990 2010 2030 GAAAAATCGAAATCTATTGTCTATCTCCTCAATTTGGATTGGATTTTCTGCATATCATCG 2050 2070 2090 CTCTAGATTTCGCGGGTTTTGGATTCGATTCCTTACCCTTCTCCAATCGGTAAGAACAAG 2110 2130 2150 CTCCAAAGTTTGTTCCTTTTTTTCAATTTTCGCCAATTCTGTAATCTCATCATTGTTCTT 2170 2190 2210 GTTTGATTTGGATGCAGAAGTTTTTGGGTTTGAATTGGATTTGGGTTTCGTTCCAAAATC 2230 2250 2270 AGCTCTTTTTGTTAATCAGGTGAGTTTTTAGGTATTTGAATCTCCAATTGCTTCCCTTGC 2290 2310 2330 AATGACTAAGTATTGTGAAATGTTTAGGGTTTCATCTGTGTGGGTCTTGTTTTGAAGCAA 2350 2370 2390 TTTGTGTGTGTTTGGATGAAAGTAGCAGATATGCAGGACCAGCTGGTGTGTCATGGTTGT 2410 2430 2450 AGGAATTTATTGATGTATCCTAGAGGAGCATCTAATGTGCGTTGTGCGTTATGTAACACT 2470 2490 2510 ATCAACATGGTTCCTCCTCCTCCTCCACCTCACGGTATCGATTTCTTTGTTGAATTTGAA 2530 2550 2570 TTGAGGATGAGGTTAATATGCTCTGCAATTGTATTATAACTTGGGTTCTGATTCTGAATA 2590 2610 2630 CAGACATGGCACACATTATATGTGGTGGTTGTAGAACAATGCTTATGTATACGCGTGGGG 2650 2670 2690 CTAGTAGCGTAAGATGCTCTTGCTGTCAAACTACGAACCTTGTGCCAGGTATATTAATAA 2710 2730 2750 TATCGTGACATCCATATCAATCCTTTTAAAGACCATGTATTATATTGCTTTATAAGGTCT 2770 2790 2810 TTTAGTCCTTTAGAATCTTCTTTCACACTTTTGTTTGATAACATTGTTCTGTGGAGATGA 2830 2850 2870 TGCTTACGTAACGTATTTCCACTTTTCCCAAAGATGTATATGAATCTGAATTCTGAAAAT 2890 2910 2930 ATCTGGGATTTGTAAAGCAGCTGAAAGTACTTAAAACAAAGCTTTTAGATGGTCCCGGTG 2950 2970 2990 GACTAGGTAACTACTTGTTAGAGCTAGTAGGGTTTATTATTGTTTTGTTTGATCTACCAT 3010 3030 3050 TAGATTCTTATCTTTAATTAGCGTCTAAGCTGTTGTCATTTAGCTGTATGATTATCATTT 3070 3090 3110 ATCCATGACTGCTTAAGAACATTGCTGATTACTTCGTTCATTAGTATTTCTTGGATTTTT 3130 3150 3170 CTAGCATTAACATTGCTTGTTTTCTGAATCTGTGCGTGTCTTTTTTGAAATCGACAGCGC 3190 3210 3230 ACTCCAATCAGGTTGCCCATGCTCCTTCCAGTCAGGTTGCGCAAATCAATTGTGGGCATT " 3250 3270 3290 GTCGGACGACCCTCATGTATCCTTACGGTGCATCATCCGTCAAATGCGCTGTTTGTCAAT 3310 3330 3350 TCGTAACTAACGTTAATGTGATTATTCCTATCTATTAAGCCACCTCTGCATGGTTGAGTT 3370 3390 3410 AAGTATAGAGATCTTTCTGTTGGAAATTTTCATTTCTGATTCATTTTGCATCCTTAGATG 3430 3450 3470 AGCAATGGAAGGGGTACCTCTCCCAACTAACCGGCCAAATGGAACAGCTTGTCCCCCCTC 3490 3510 3530 TACATCAACTGTGAGTTATCAAATTATGAATTTGTAATAGTTCTGTATATTCTTATGGAA 3550 3570 3590 CTGGTACTTACTCTGTTCATCGATTTTTCATTTTACCAACAGTCAACACCACCCTCTCAG 3610 3630 3650 ACCCAAACCGTTGTTGTAGAAAACCCCATGTCCGTTGATGAAAGCGGAAAGTTGGTGAGT 3670 3690 3710 ATTTCTATCACCTGTGTTCTTCTTCTTATTTACCACATTAGAGGAAGATATGACAAAGTG 3730 3750 3770 ACTGAAACACACAAATTGCAGGTGAGCAATGTTGTTGTTGGAGTGACAACTGACAAAAAG 3790 3810 3830 TAATCAAGAATGAGTGAGATCTTAAAGATCAAATCCAAATTCTTCCTCTATTCCTGCGTT 3850 3870 3890 TGGTTTGTGCATATTACATACGCGGAAAAACTGTATGTTATATATCTCTTGACTCCTTTT 3910 3930 3950 TAACCCAAGAGAAAAAGCTTATCAGAATCTCTTGTTACTGCATTATTGGGGTTTATTCAA 3970 3990 4010 AGTTGAAGACACAAGGTTTTTGCTCGAATAATTTGGCATTCTTTTGCTCCATGGAACTTG 4030 4050 4070 ACCTTCTCTTCTGTTAGTTGACTTCTAAAACTCCATCGGCCCTTGTGGCATTGTTAATGT 4090 4110 4130 ATGTATGAATATAATCTGATACACCAACCAATCATTAAGATTTGGGTTTGAAATCTGTCT 4150 4170 4190 CTTCCGTGGATGAGATATGCTACATGTCACAAGAACTGGTCTTAGCTTTGGTAGATAAGA 4210 4230 4250 CTTGTCTTAGAAGCAAGTCTTGAAATCTGGAAATCTATTTTGCAGTAATCTTGTCACAAC 4270 4290 4310 AACCATAACCTAATCAGTCAGTACCCTCCAAGAAACATTAAAGTTAGATGATCCGACAAA 4330 4350 4370 ACCTCTCAACAAAACCAACTCTTTCCATATAAATACTCTTTAACACTGGACCAAATTTNC 4390 4410 4430 ACCCTTCCTCTTGATCCTCCCTGCATCACAATGGCCAAAAAAAAAATGGTGGTTGGCNGG 4450 4470 4490 TGGGTACCACAAAGAGCTGGAAACTACTCTTGGGGCTGAGAATATTTGCATTCATGGCTA 4510 CTTTAGCTGCAG SEQ ID NO:14 10 30 50 CTTACGCGTCATGTAAAAAAAAAAGAAGCGTAAATTACGAAAAACAGAGAGATAAATCCG 70 90 110 GGCATTGAGATTTTGGAGATAGAGAGAGAGAAAAATCGAAATCTATTGTCTATCTCCTCA 130 150 170 ATTTGGATTGGATTTTCTGCATATCATCGCTCTAGATTTCGCGGGTTTTGGATTCGATTC 190 210 230 CTTACCCTTCTCCAATCGAAGTTTTTGGCTTTGAATTGGATTTGGGTTTCGTTCCAAAAT 250 270 290 CAGCTCTTTTTGTTAATCAGATATGCAGGACCAGCTGGTGTGTCATGGTTGTAGGAATTT 310 330 350 ATTGATGTATCCTAGAGGAGCATCTAATGTGCGTTGTGCGTTATGTAACACTATCAACAT 370 390 410 GGTTCCTCCTCCTCCTCCACCTCACGACATGGCACACATTATATGTGGTGGTTGTAGAAC 430 450 470 GATGCTTATGTATACGCGTGGGGCTAGTAGCGTAAGATGTTCTTGCTGTCAAACTACGAA 490 510 530 CCTTGTGCCAGCGCACTCCAATCAGGTTGCCCATGCTCCTTCCAGTCAGGTTGCGCAGAT 550 570 590 CAATTGTGGGCATTGTCGGACGACCCTCATGTATCCTTACGGTGCATCATCCGTCAAATG 610 630 650 CGCTGTTTGTCAATTCGTAACTAACGTTAATATGAGCAATGGAAGGGTACCTCTCCCAAC 670 690 710 TAACCGGCCAAATGGAACAGCTTGTCCCCCCTCTACATCAACTTCAACACCACCCTCTCA 730 750 770 GACCCAAACCGTTGTTGTAGAAAACCCCATGTCCGTTGATGAAAGCGGAAAGTTGGTGAG 790 810 830 CAATGTTGTTGTTGGAGTGACAACTGACAAAAAGTAATCAAGAATGAGTGAGATCTTAAA 850 870 890 GATCAAATCCAAATTCTTCCTCTGTTCCTGCGTTTGGTTTGTGCATATTACATACGCGGA 910 930 950 AAAACTGTATGTTATATATCTCTTGACTCCTTTTTAACCCAAGAGAAAAAGCTTATCAGA 970 AAAAAAAAAAAAAAAAA SEQ ID NO:15 10 30 50 GAAATCTATTGTCTATCTCCTCAATTTGGATTGGATTTTCTGCATATCATCGCTCTAGCT 70 90 110 TTCGCGGGTTTTGGATTCGATTCCTTACCCTTCTCCAATCGAAGTTTTTGGCTTTGAATT 130 150 170 GGATTTGGGTTTCGTTCCAAAATCAGCTCTTTTTGTTAATCAGGGTTTCATCTGTGTGGG 190 210 230 TCTTGTTTTGAAGCAATTTGTGTGTGTTTGGATGAAAGTAGCAGATATGCAGGACCAGCT 250 270 290 GGTGTGTCATGGTTGTAGGAATTTATTGATGTATCCTAGAGGAGCATCTAATGTGCGTTG 310 330 350 TGCGTTATGTAACACTATCAACATGGTTCCTCCTCCTCCTCCACCTCACGACATGGCACA 370 390 410 CATTATATGTGGTGGTTGTAGAACAATGCTTATGTATACGCGTGGGGCTAGTAGCGTAAG 430 450 470 ATGCTCTTGCTGTCAAACTACGAACCTTGTGCCAGCGCACTCCAATCAGGTTGCCCATGC 490 510 530 TCCTTCCAGTCAGGTTGCGCAGATCAATTGTGGGCATTGTCGGACGACCCTCATGTATCC 550 570 590 TTACGGTGCATCATCCGTCAAATGCGCTGTTTGTCAATTCGTAACTAACGTTAATATGAG 610 630 650 CAATGGAAGGGTACCTCTCCCAACTAACCGGCCAAATGGAACAGCTTGTCCCCCCTCTAC 670 690 710 ATCAACTTCAACACCACCCTCTCAGACCCAAACCGTTGTTGTAGAAAACCCCATGTCCGT 730 750 770 TGATGAAAGCGGAAAGTTGGTGAGCAATGTTGTTGTTGGAGTGACAACTGACAAAAAGTA 790 810 830 ATCAAGAATGAGTGAGATCTTAAAGATCAAATCCAAATTCTTCCTCTATTCCTGCGTTTG 850 870 890 GTTTGTGCATATTACATACGCGGAAAAACTGTATGTTATATATCTCTTGACTCCTTTTTA 910 930 950 ACCCAAGAGAAAAAGCTTATCAGAATCTCTTGTTACTGCATTATTGGGGTTTATTCAAAG 970 990 TTGAAGACACAAGGTTTTTGCTCGAAAAAAAAAAAAAAAAAAAAAA SEQ ID NO:16 MetGlnAspGlnLeuValCysHisGlyCysArgAsn euLeuMetTyrProArgGlyAla 10 20 SerAsnValArgCysAlaLeuCysAsnThrlleAsnMetValProProProProProPro 30 40 HisAspMetAlaHisIlelleCysGlyGlyCysArgThrMet euMetTyrThrArgGly 50 60 AlaSerSerValArgCysSerCysCysGlnThrThrAsn euValProAlaHisSerAsn 70 80 GlnValAlaHisAlaProSerSerGlnValAlaGlnlleAsnCysGlyHisCysArgThr 90 100 Thr euMetTyrProTyrGlyAlaSerSerValLysCysAlaValCysGlnPheValThr 110 120 AsnValAsnMetSerAsnGlyArgValProLeuProThrAsnArgProAsnGlyThrAla 130 140 CysProProSerThrSerThrSerThrProProSerGlnThrGlnThrValValValGlu 150 160 AsnProMetSerValAspGluSerGlyLysLeuValSerAsnValValValGlyValThr 170 180 ThrAspLysLys SEQ ID NO:17 MetLysValAlaAspMetGlnAspGlnLeuValCysHisGlyCysArgAsnLeuLeuMet 10 20 TyrProArgGlyAlaSerAsnValArgCysAlaLeuCysAsnThrlleAsnMetValPro 30 40 ProProProProProHisAspMetAlaHisIlelleCysGlyGlyCysArgThrMetLeu 50 60 MetTyrThrArgGlyAlaSerSerValArgCysSerCysCysGlnThrThrAsnLeuVal 70 80 ProAlaHisSerAsnGlnValAlaHisAlaProSerSerGlnValAlaGlnlleAsnCys 90 100 GlyHisCysArgThrThrLeuMetTyrProTyrGlyAlaSerSerValLysCysAlaVal 110 120 CysGlnPheValThrAsnValAsnMetSerAsnGlyArgValProLeuProThrAsnArg 130 140 ProAsnGlyThrAlaCysProProSerThrSerThrSerThrProProSerGlnThrGln 150 160 ThrValValValGluAsnProMetSerValAspGluSerGlyLysLeuValSerAsnVal 170 180 ValValGlyValThrThrAspLysLys SEQ ID NO: 18 5'-CAG TGG ATC TTT CCT CAG ACG-3' SEQ ID NO: 19 5'-CAT CTT CTT CTG CAA TCT GGG-3' SEQ ID NO:20 5 '-CAT CCA TCA AAC AAA CTC C-3' SEQ ID NO:21 5'-TGT TTC AGA GTA GCC AAT TC-3' SEQ ID NO:22 5'-CAC GTT AGT TAG TTA GAA GG-3' SEQ ID NO:23 5' -CTG ATG TTC TCT AC A AAT GG-3' SEQ ID NO:24 10 5'-CGT ATC CGC ATT TCT TCA CTG C-3' SEQ ID NO:25 5'-CAT CTG CAA CAT CTT CCC CAG-3' SEQ ID NO:26 5'-TTG AGT CCT TCT TGT CTG-3' SEQ ID NO:27 5'-CTA GAG CTT GAA AGT TGA TG-3' SEQ ID NO:28 5'-GAA TGG TGT AAC CAA ACT C-3' SEQ ID NO:29 5 '-CAT ACC GTA TGA TGG AAC-3' SEQ ID NO:30 5' -GAA CTC ATT GTA TGG ACC-3' SEQ ID NO:31 5'-CTA AGA TGG GAA TGT TGG-3' SEQ ID NO:32 5'-CCA AGA AGA GAA AAC GGA GA-3' SEQ ID NO:33 5'-AAC AAT AGG AGG TGC AGA GT-3' SEQ ID NO:34 5'-ACC TAA CAAAAA GAAAAG TGT GTGAGG-3' SEQ ID NO:35 5'-ATA ATA AAC CCT ACT AGC TCT AAC AAG-3' SEQ ID NO:36 5'-CTG CTA CTT TCA TCC AAA C-3' 11 SEQ ID NO:37 5'- GTA AAA CGA CGG CCA TG -3' SEQ ID NO:38 5'- GGA AAC AGC TAT GAC CAT G -3' SEQ ID NO:39 5'- TTC ATG GCAATG GTGTGA CCC C -3' SEQ ID NO:40 5'- CTG CCG GAT TCT TGA TCG AAG A -3' SEQ ID NO:41 5'- AGA GGA AGG TCC GCC TCC GG -3' SEQ ID NO:42 5'- CTC TGC TCT CCT GAG ACT GCT T -3' SEQ ID NO:43 5'- CAT CAT AAT GTC TCC TTT TGA GAC -3' SEQ ID NO:44 5'- GCC ATC CAT TAT TCA TCG CCT -3' SEQ ID NO:45 5'- GAG GAG GAA GAA CTG CAG ATT CC -3' SEQ ID NO:46 5'- GTG CTC CAT GTC CAA ATC ATA C -3' SEQ ID NO:47 10 30 50 AATATATCGAAACGAGATTCCACAATTAGTCTCTAGTCAAAGAGCTTCATGGCAATGGTG 70 90 110 2 TGACCCCAAATATAGATTTGATGAAAGTGAGGAAATAGGAGAAGAAATGAAGAACACAGG 130 150 170 ATGTGTCTTCTTCTTCTAAGTCACTAACAAAATCAACAAAGAGGAGAAGCCATTATTATA 190 210 230 TAATAGAGAGATTGAGAGAAGAGATTTATCCAAAAAAATATTGCAATTCTTCTTGGAGTG 250 270 290 AATAATGCCAGTCCCTCTTGCACCATATCCAACACCTCCGGCACCGGCACAGGCTCCGTC 310 330 350 GTACAACACTCCTCCGGCAAATGGAAGTACAAGTGGGCAGAGCCAGTTAGTGTGTTCAGG 370 390 410 TTGCAGAAACCTTCTGATGTATCCCGTCGGAGCAACCTCCGTCTGCTGCGCCGTCTGTAA 430 450 470 CGCCGTCACGGCCGTTCCTCCGCCGGGAACGGAGATGGCACAGTTAGTATGTGGAGGATG 490 510 530 CCATACACTCTTAATGTACATTCGTGGAGCTACAAGTGTTCAATGTTCTTGTTGTCACAC 550 570 590 TGTTAATCTCGCCCTCGAAGCGAACCAAGTAGCGCATGTGAATTGCGGAAACTGCATGAT 610 630 650 GCTACTAATGTATCAATATGGAGCAAGATCAGTGAAATGTGCCGTTTGTAACTTTGTCAC 670 690 710 ATCTGTTGGGGGTTCAACGAGCACGACTGATTCGAAGTTTAACAATTAAAACTTGGATCT 730 750 770 ATCTACCTATCAATATCTATTGAGTTATGAGCAATATAGAGGAAGCATCAAATCTTTTTC 790 810 830 ACTCTCTCTTCGATCAAGAATCCGGCAGTTATGAGTTTGAAACCATTTTCGGAAGTAAAT 850 870 890 GAAATATGTAATTCGTCGAAATTTCTGACTTTGGTCTCTTTGTCCGTTTGTATAGAGCTA 910 AAAAAAAAAA SEQ ID NO: 48 MetProValProLeuAlaProTyrProThrProProAlaProAlaGlnAlaProSerTyr 10 20 AsnThrProProAlaAsnGlySerThrSerGlyGlnSerGlnLeuValCysSerGlyCys 3 30 40 ArgAsnLeuLeuMetTyrProValGlyAlaThrSerValCysCysAlaValCysAsnAla 50 60 ValThrAlaValProProProGlyThrGluMetAlaGlnLeuValCysGlyGlyCysHis 70 80 ThrLeuLeuMetTyrlleArgGlyAlaThrSerValGlnCysSerCysCysHisThrVal 90 100 AsnLe iAlaLeuGluAlaAsnGlnValAlaHiεsValAsnCysGlyAsnCysMetMetLeu 110 120 LeuMetTyrGlnTyrGlyAlaArgSerValLysCysAlaValCysAsnPheValThrSer 130 140 ValGlyGlySerThrSerThrThrAspSerLysPheAsnAsn 150 SEQ ID NO: 49 CysSerGlyCysArgAsnLeuLeuMetTyrProValGlyAlaThrSerValCysCysAlaValCys SEQ ID NO: 50 CysGlyGlyCysHisThrLeuLeuMetTyrlleArgGlyAlaThrSerValGlnCysSerCysCys SEQ ID NO: 51 CysGlyAsnCysMetMetLeuLeuMetTyrGlnTyrGlyAlaArgSerValLysCysAlaValCys SEQ ID NO: 52 CysXxxXxxCysArgXxxXxxLeuMetTyrXxxXxxGlyAlaSerXxxValXxxCysXxxXxxCys SEQ ID NO: 53 CysXxxXxxCysXxxXxxLeuLeuMetTyrXxxXxxGlyAlaXxxSerValXxxCysXxxXxxCys SEQ ID NO:54 10 30 50 GAGGAGGAAGAGGAAGGTCCGCCTCCGGGATGGGAATCTGCAGTTCTTCCTCCTCCAATC 70 90 110 GTCACCATCACCGCCGCCGTAAACCCCAATCCCACCACCGTAGAAATTCCCGAAAAGGCC 4 130 150 170 CAAATGGTATGTGGATCTTGCAGGCGTTTGCTTTCTTATCTAAGAGGATCCAAACATGTT 190 210 230 AAGTGCTCCTCTTGTCAGACTGTTAATCTCGTTCTTGAAGCTAACCAGGTTGGTCAGGTG 250 270 290 AATTGCAACAATTGCAAACTGCTACTGATGTATCCTTATGGAGCTCCAGCTGTTAGATGT 310 330 350 TCCTCCTGCAATTCTGTCACAGATATCAGTGAAAACAACAAACGACCTCCATGGTCTGAG 370 390 410 CAGCAAGGACCACTCAAAAGTTTAAGCAGTCTCAGGAGAGCAGAGAATTAAACTTGAACC 430 450 470 GATTTTTGTCAATTTTGAACCGGTTTGACGACTAAAAACCTTGTAATAATGTCGAAGGAT 490 AGATGAAATAAAATCACACC SEQ ID NO:55 GluGluGluGluGluGlyProProProGlyTrpGluSerAlaValLeuProProProIle 10 20 ValThrlleThrAlaAlaValAsnProAsnProThrThrValGluIleProGluLysAla 30 40 GlnMetValCysGlySerCysArgArgLeuLeuSerTyrLeuArgGlySerLysHisVal 50 60 LysCysSerSerCysGlnThrValAsnLeuValLeuGluAlaAsnGlnValGlyGlnVal 70 80 AsnCysAsnAsnCysLysLeuLeuLeuMetTyrProTyrGlyAlaProAlaValArgCys 90 100 SerSerCysAsnSerValThrAspIleSerGluAsnAsnLysArgProProTrpSerGlu 110 120 GlnGlnGlyProLeuLysSerLeuSerSerLeuArgArgAlaGluAsn 55 SEQ ID NO:56 CGSCRRLLSYLRGSKHVKCSSC 15 SEQ ID NO:57 CNNCKLLLMYPYGAPAVRCSSC SEQ ID NO: 58 10 30 50 GGAAGAGATACAACAACAAACGCAGAAGGAAGAACAAAAGCACCGTGAAGAAGAAGAGGA 70 90 110 GGAAGAGGAAGGTCCGCCTCCGGGATGGGAATCTGCAGTTCTTCCTCCTCCAATCGTCAC 130 150 170 CATCACCGCCGCCGTAAACCCCAATCCCACCACCGTAGAAATTCCCGAAAAGGCCCAAAT 190 210 230 GGTATGTGGATCTTGCAGGCGTTTGCTTTCTTATCTAAGAGGATCCAAACATGTTAAGTG 250 270 290 CTCCTCTTGTCAGACTGTTAATCTCGTTCTTGAAGCTAACCAGGTTGGTCAGGTGAATTG 310 330 350 CAACAATTGCAAACTGCTACTGATGTATCCTTATGGAGCTCCAGCTGTTAGATGTTCCTC 370 390 410 CTGCAATTCTGTCACAGATATCAGTGTATGTATTCACAGATGGTTTTGTGCTCCATGTCC 430 450 470 AAATCATACTTGGAAGAGTTGATACATTTTGAGATCCGAGTAAGTAATCATCTGATGAAT 490 510 530 CATTTATAATAAACTGTGTTATATTTCAGGAAAACAACAAACGACCTCCATGGTCTGAGC 550 570 590 AGCAAGGACCACTCAAAAGTTTAAGCAGTCTCAGGAGAGCAGAGAATTAAACTTGAACCG 610 630 650 ATTTTTGTCAATTTTGAACCGGTTTGACGACTAAAAACCTTGTAATAATGTCGAAGGATA 670 690 GATGAAATAAAATCACCATTAATAATCTAAAAAAAAAAAAAAAA SEQ ID NO:59 10 30 50 CTCTATCCTTACTTCAACGGAGCTTTACCAGACCCAAACTCTCTTAGGCCGCACCGAGAG 70 90 110 TTGTTTGTACGTGTGCTTAACGCAGATTACATATGACGCTTCTAACCCACAATTAATTTG 130 150 170 GTTCACTCTTTGCCGCAAACCAAATAGCTCAAAAAAGATTTTAATCCCAATTTCATATCC 190 210 230 TAAATCTGCATCATGGTCGGATAGTGTAGTGGCTGTTGGTCCTAATATCTACGCTATTGG 250 270 290 GGGATTCAGTAATAATAGAACTAAACCTTCGTCTAGCGTCATGGTCATGGATTGTCGTAC 310 330 350 TCACACATGGTGTGAGGCCCCTAGCATGCAGGTTTCCCGTGTGTTCCAATCTACTTGCGT 370 390 410 CCTTGATGGGAAAATATATGTAACAGGAGGCCGCGGAACTCTCGATTCAACGAAATGGAT 430 450 470 GGAGGTTTTTGATACGAAAACCCAAACTTGGGAGTTTTTGCAATTCCCGAGTGAGGAGAA 490 510 530 GATATGCACAGGCTATAAGTGTGAGAGCATAGTGTATGAAGGAACTGTCTATGTAAGGTC 550 570 590 GTATTTTCATAATGTGACTTACAAGCTGCATAAAGGTAGATGGATTCAGCGGCAGACTTT 610 630 650 AGGCGATGAATAATGGATGGCCGTTGCTCATCATTTTTTTGTGTGATAAAGAACGTGTTC 670 690 710 TACTTGTTGCAATAGAAGTGGTAACGGTATGATCGATTGGTATGACTCGGAAAAAGGATC 730 750 770 ATGGACAACTATGAAGGGGTTGGAAAGATTGCCTAAAGTTTATGGTAATGTTAAATTGGC 790 810 830 ATATTATGGTGGAAAAATGGTGGTGGTGTACGTGGAGTGCTAAGGAGTGGGGTAACGTGA 850 870 890 GAAAAATTTGGTGTGCGGAAATTACGATTGAAAAACGCAAGGATGGAGAGATTTGGGGGA 910 930 950 TACTAGAATGGTTTGACGATGTATATAAAGCCAAGGATGAGCTAGAATATTTAGCTGTAG 970 990 1010 TGCATGCTGTTGTTACTACCATCTGATTGATAAGAGAGTCATGTGAACATTGTTCATTGA 1030 1050 1070 TTCACCGATGCAATAACGAATTTATCTACTATCATTTGTTTTGATTTTCTTTCTAAATCT 1090 1110 1130 TTTTTGTTTGTTCTTGTATTGAATTTTACCTTACATTTATTAAGAAAGTCAACTATTTGT 1150 1170 1190 CAACGTTACTGGAAAGTTAAAAAGGTAAAAGTAATAATAATCTGAGAGTTAACTTTGGAC 1210 1230 1250 ATCTTCGCCGGAGCCGAGACGGAAGGCGTGATGGAAGAGATACAACAACAAACGCAGAAG 1270 1290 1310 GAAGAACAAAAGCACCGTGAAGAAGAAGAGGAGGAAGAGGAAGGTCCGCCTCCGGGATGG 1330 1350 1370 GAATCTGCAGTTCTTCCTCCTCCAATCGTCACCATCACCGCCGCCGTAAACCCCAATCCC 1390 1410 1430 ACCACCGTAGAAATTCCCGGTATTCTTGTAGTCTTGTCTATTTTAGGGTTTATCGATTTG 1450 1470 1490 CTTCCATTTCTTGCTACAGTCTGATCAAATTAGAGATTTTTAGTGGAGTTTGTAGACTTT 1510 1530 1550 TAGAGATAACCCATTTTCGATTCCGAGAATTGATTAGTGTTTTTTTTCTGCAAATCTTCT 1570 1590 1610 TTGTTTTTGGGGTTGTTGCAGAAAAGGCCCAAATGGTATGTGGATCTTGCAGGCGTTTGC 1630 1650 1670 TTTCTTATCTAAGAGGATCCAAACATGTTAAGTGCTCCTCTTGTCAGACTGTTAATCTCG 1690 1710 1730 TTCTTGAAGGTTCGTTCTTCCATGGCTTTTTTATCTCTTATTCATTACTTGAAAAGCTTT 1750 1770 1790 TGTTGATAATCTCAGTCACTTGAAACTCTTAATGGAACAATCTTGGAATGCTCTCTCAGT 1810 1830 1850 CTAGTTTTACTTAGCATGTGTGAATGATATATCTATGTTCTTTTGAGAATCTCAAAATGT 1870 1890 1910 AAGCTTCCTGAGACCAAATGAGTTTAGTTCTTAACTGACACAAGAATGATCTTTGGTTAG 1930 1950 1970 GATTCTTCTCTTAAGCTTTTGTGAGCCTTTTGGTCTCTACTCCATCATAATGTCTCCTTT 1990 2010 2030 GTAGACCATTTATGTGGTCTTTATCCTTTACTCTTACTACTCTTGGGGAAATTGTGTGAT 2050 2070 2090 CTTAAGACCAAGATTGTTCTTCTTAGCTTGTGAATCACTTGGCCTCATTATTGATGAAAT 2110 2130 2150 AGCCTTCTTCTCTTATCGGTTCTGGACTTGTCGTTCTTTGTTTGCAGCTAACCAGGTTGG 2170 2190 2210 TCAGGTGAATTGCAACAATTGCAAACTGCTACTGATGTATCCTTATGGAGCTCCAGCTGT 2230 2250 2270 TAGATGTTCCTCCTGCAATTCTGTCACAGATATCAGTGTATGTATTCACAGATGGTTTTG 2290 2310 2330 TGCTCCATGTCCAAATCATACTTGGAAGAGTTGATACATTTTGAGATCCGAGTAAGTAAT 2350 2370 2390 CATCTGATGAATCATTTATAATAAACTGTGTTATATTTCAGGAAAACAACAAACGACCTC 2410 2430 2450 CATGGTCTGAGCAGCAAGGACCACTCAAAAGTTTAAGCAGTCTCAGGAGAGCAGAGAATT 2470 2490 2510 AAACTTGAACCGATTTTTGTCAATTTTGAACCGGTTTGACGACTAAAAACCTTGTAATAA 2530 2550 2570 TGTCGAAGGATAGATGAAATAAAATCACCATTAATAATCTCATTGAATTCCCATTCTTTC 2590 2610 2630 AGATATTACTTGCTCATCATCCTTTACTGTTTTAAGCTTTAGTGGTTAAAAAGAATGTGT 2650 2670 2690 ATATATCCATACAAAAGTTGATATATGTACTGGACCAATATAAACAAACACAGCTCACAG 2710 2730 2750 TCTCACACAATACATAAAAACAAAATTCATATTTCACAGGTGAGAAAAACTAACTAGTAG 2770 2790 2810 TCTACTTGGCCGAATTTGTCAATGAATTTCAATAATTAGGTCGTATAAATAGCAAACAAA 2830 2850 2870 ACATGGACTCTTACCCAACCAAATATGCATAAATAATTTACATTACAGTTTCATATAAAA 2890 2910 2930 TACAAACTAATGGTGGGTCCTCGAGAGAGCTAACAAGAGCTGTGTGTGGGTGAAGAACCA 2950 2970 2990 ACTTGTCAACGAAACCAATTTAATGGAAATCAACCCTAAATTTAATGAAACCTTGGACGA 3010 3030 3050 AACTTACATTTTGTTAACCAGTTTATCCTTTTAAATCAAACCTGCATAGAATTTTGATTT SEQ ID NO:60 MetGluGluIleGlnGlnGlnThrGlnLysGluGluGlnLysHisArgGluGluGluGlu 10 20 GluGluGluGluGlyProProProGlyTrpGluSerAlaValLeuProProProIleVal 30 40 ThrlleThrAlaAlaValAsnProAsnProThrThrValGluIleProGluLysAlaGln 50 60 MetValCysGlySerCysArgArgLeuLeuSerTyrLeuArgGlySerLysHisValLys 70 80 19 CysSerSerCysGlnThrValAsnLeuValLeuGluAlaAsnGlnValGlyGlnValAsn 90 100 CysAsnAsnCysLysLeuLeuLeuMetTyrProTyrGlyAlaProAlaValArgCysSer 110 120 SerCysAsnSerValThrAspIleSerGluAsnAsnLysArgProProTrpSerGluGln 130 140 GlnGlyProLeuLysSerLeuSerSerLeuArgArgAlaGluAsn 150 SEQ ID NO:61 MetGluGluIleGlnGlnGlnThrGlnLysGluGluGlnLysHisArgGluGluGluGlu 10 20 GluGluGluGluGlyProProProGlyTrpGluSerAlaValLeuProProProIleVal 30 40 ThrlleThrAlaAlaValAsnProAsnProThrThrValGluIleProGluLysAlaGln 50 60 MetValCysGlySerCysArgArgLeuLeuSerTyrLeuArgGlySerLysHisValLys 70 80 CysSerSerCysGlnThrValAsnLeuValLeuGluAlaAsnGlnValGlyGlnValAsn 90 100 CysAsnAsnCysLysLeuLeuLeuMetTyrProTyrGlyAlaProAlaValArgCysSer 110 120 SerCysAsnSerValThrAspIleSerValCysIleHisArgTrpPheCysAlaProCys 130 140 ProAsnHisThrTrpLysSer SEQ ID NO:62 CysXxxXxxCysXxxXxxLeuLeuXxxTyrXxxXxxGlyXxxXxxXxxValXxxCysSerSerCys SEQ ID NO: 63 LeuValCysHisGlyCysArgAsnLeuLeuMetTyrProArgGlyAlaSerAsnValArgCysAlaLeuCysA snThrlleAsnMetVal IlelleCysGlyGlyCysArgThrMetLeuMetTyrThArgGlyAlaSerSerValArgCysSerCysCysG InThrThrAsnLeuVal 20 IleAsnCysGlyHisCysArgThrThrLeuMetTyrProTyrGlyAlaSerSerValLysCysAlaValCysG InPheValThrAsnVal SEQ ID NO: 64 LeuValCysSerGlyCysArgAsnLeuLeuMetTyrProValGlyAlaThrSerValCysCysAlaValCysA snAlaValThrAlaVal LeuValCysGlyGlyCysHisThrLeuLeuMetTyrlleArgGlyAlaThrSerValGlnCysSerCysCysH isThrVa1 snLeuAla ValAsnCysGlyAsnCysMetMetLeuLeuMetTyrGlnTyrGlyAlaArgSerValLysCysAlaValCysA snPheValThrSerVal SEQ ID NO: 65 MetValCysGlySerCysArgArgLeuLeuSerTyrLeuArgGlySerLysHisValLysCysSerSerCysG InThrValAsnLeuVal ValAsnCysAsnAsnCysLysLeuLeuLeuMetTyrProTyrGlyAlaProAlaValArgCysSerSerCysA snSerValThrAspIle SEQ ID NO: 66 Nucleic acid sequence of C 10 30 50 AGCAACAACAACAACAACCAGCAACCACCACCAACCTCCGTCTATCCACCTGGCTCCGCC 70 90 110 GTCACAACCGTAATCCCTCCTCCACCATCTGGATCTGCATCAATAGTCACCGGAGGAGGA 130 150 170 GCGACATACCACCACCTCCTCCAGCAACAACAGCAACAGCTTCAAATGTTCTGGACATAC 190 210 230 CAGAGACAAGAGATCGAACAGGTAAACGATTTCAAAAACCATCAGCTCCCTCTAGCTCGT 250 270 290 ATCAAAAAAATCATGAAAGCTGATGAAGATGTGCGTATGATCTCCGCCGAAGCACCGATT 310 330 350 CTCTTCGCGAAAGCTTGTGAGCTTTTCATTCTCGAACTTACGATTAGATCTTGGCTTCAC 370 390 410 GCTGAAGAGAACAAACGTCGTACGCTTCAGAAAAACGATATCGCTGCTGCGATTACTAGA 430 450 470 ACCGATATCTTCGATTTCCTTGTTGATATTGTTCCTAGGGAAGAGATCAAGGAAGAGGAA 490 510 530 GATGCAGCATCGGCTCTTGGTGGAGGAGGTATGGTTGCTCCCGCCGCGAGCGGTGTTCCT 1 550 570 590 TATTATTATCCACCGATGGGACAACCGGCGGTTCCTGGAGGGATGATGATTGGAAGACCG 610 630 650 GCGATGGATCCTAGCGGTGTTTATGCTCAGCCTCCTTCTCAGGCATGGCAAAGCGTTTGG 670 690 710 CAGAATTCAGCTGGTGGTGGTGATGATGTGTCTTATGGAAGTGGAGGAAGTAGCGGCCAT 730 750 770 GGTAATCTCGATAGCCAAGGTTGAGCTATGGAACCAGAAGCTTAGAGATTTAATCATCAT 790 810 830 TTCGACCCTGCAAGTGTCTGATTCTTATATGTCTATGATTCGAATGACTTA SEQ ID NO: 67 Amino acid sequence of C SerAsnAsnAsnAsnAsnGlnGlnProProProThrSerValTyrProProGlySerAla 10 20 ValThrThrVal lleProProProProSerGlySerAlaSerlleValThrGlyGlyGly 30 40 AlaThrTyrHisHisLeuLeuGlnGlnGlnGlnGlnGlnLeuGlnMetPheTrpThrTyr 50 60 GlnArgGlnGluIleGluGlnValAsnAspPheLysAsnHisGlnLeuProLeuAlaArg 70 80 IleLysLysIleMetLysAlaAspGluAspValArgMetlleSerAlaGluAlaProIle 90 100 LeuPheAlaLysAlaCysGluLeuPhelleLeuGluLeuThrlleArgSerTrpLeuHis 110 120 AlaGluGluAsnLysArgArgThrLeuGlnLysAsnAspI leAlaAlaAlalleThrArg 130 140 ThrAspIlePheAspPheLeuValAspIleValProArgGluGluIleLysGluGluGlu 150 160 AspAlaAlaSerAlaLeuGlyGlyGlyGlyMetValAlaProAlaAlaSerGlyValPro 170 180 TyrTyrTyrProProMetGlyGlnProAlaValProGlyGlyMetMetlleGlyArgPro 190 200 AlaMetAspProSerGlyValTyrAlaGlnProProSerGlnAlaTrpGlnSerValTrp 210 220 2 GlnAsnSerAlaGlyGlyGlyAspAspValSerTyrGlySerGlyGlySerSerGlyHis 230 240 GlyAsnLeuAspSerGlnGly SEQ ID NO: 68 Nucleic acid sequence of CC 10 30 50 AGTATGGATGAGCTTTCAGAAGCTTCTCAGATACTCACATGTTGCTCTGACATGGTGTAC 70 90 110 TGCACGGTTTGCGCATGTATGCAGACACAACACAAGATGGAAATGGACAAGAGGGACGGT 130 150 170 AAGTTCGGGCCACAGCCAATGGCAGTGCCTCCGGCTCAGCAAATGTCACGGTTTGATCAA 190 210 230 GCCACCCCACCCGCAGTCGGTTATCCTCCACAACAAGGTTATCCACCTTCTGGTTATCCT 250 270 290 CAACACCCTCCACAAGGTTATCCACCTTCTGGCTATCCTCAAAACCCTCCTCCCTCAGCT 310 330 350 TATTCTCAATACCCTCCTGGGGCTTATCCTCCTCCTCCCGCTTACCCAAAGTGATCACTC 370 390 410 TTTGCCTGTTTTCTCTCCCGATTGGAAAATTTTATTTCATCTTTTTTTAATGCTGTCTTG 430 450 470 TTACGGGTCAAGAATTGAACGTTCGCTGATTGTTTTGAGGTCGTTGTTTGTATGAGATTT 490 510 530 TGACCTCGCATGTTGTTGTTGTTTTCTGAAACGTCCCTCTTGGACTAAGAGATTTCATGA 550 CTTAAAAAAAAAAAAAAAAAA SEQ ID NO: 69 Amino acid sequence of CC SerMetAspGluLeuSerGluAlaSerGlnlleLeuThrCysCysSerAspMetValTyr 10 20 CysThrValCysAlaCysMetGlnThrGlnHisLysMetGluMetAspLysArgAspGly 3 30 40 LysPheGlyProGlnProMetAlaValProProAlaGlnGlnMetSerArgPheAspGln 50 60 AlaThrProProAlaValGlyTyrProProGlnGlnGlyTyrProProSerGlyTyrPro 70 80 GlnHisProProGlnGlyTyrProProSerGlyTyrProGlnAsnProProProSerAla 90 100 TyrSerGlnTyrProProGlyAlaTyrProProProProAlaTyrProLys 110 SEQ ID NO: 70 Nucleic acid sequence of FF 10 30 50 AGGTTTCCGACGTTGATGACCCAATTTCCGTCGTCGACGAAGACGATTCCGGCATCGTAT 70 90 110 TTGCTTCCGTTACAATGGCCTCAGCCGCAGAACGAGGAGATTCTTCTCGCCATGGAAGAA 130 150 170 GCTGAGTTCGAAGAAAAGTGCAACGAGATCAGAAAGATGAGTCCTGCTTTACCGGTAATT 190 210 230 GGAAAACCAGTCGTCAACAACGAACAAGAAGAGGATGATAATGAATCAGAGGATGATGAT 250 270 290 GCAGATAATGCAGAGGAATCAGATGGTGAAGAGTTTGAGCAAGAAACCGGATAAATAATC 310 330 350 TTGAGGCCGAAAATACACAAGGGTTATTGATGGCATTGGCTTGAAACTTGAGGACCCTTA 370 390 410 TCTAAATCTTCTTGTGATAAAACGACTGTGATTCTGACTTTGTAAACCANGTTTTTTTCT 430 450 470 TTTCTTAGGAACGACTGAAATGTTCACTTTTGGCCCTAAGGTTAGTCAGTGGATTATTCG 490 510 530 TAGTTAATTGTCTCAATCTCATGGTGTTAATTGTGTTAGTGTATTGACATTGAATTTTAT 550 570 GGTTTATAGATTGTAGTGATTTGATGAAAAAAAAAAAAAAAAAAAAA 24 SEQ ID NO: 71 Amino acid sequence of FF ArgPheProThrLeuMetThrGlnPheProSerSerThrLysThrlleProAlaSerTyr 10 20 LeuLeuProLeuGlnTrpProGlnProGlnAsnGluGluIleLeuLeuAlaMetGluGlu 30 40 AlaGluPheGluGluLysCysAsnGluIleArgLysMetSerProAlaLeuProVallle 50 60 GlyLysProValValAsnAsnGluGlnGluGluAspAspAsnGluSerGluAspAspAsp 70 80 AlaAspAsnAlaGluGluSerAspGlyGluGluPheGluGlnGluThrGly 90 SEQ ID NO: 72 Nucleic acid sequence of GG 10 30 50 AGGGAAACAATGAGCCAGTACAATCAACCTCCCGTTGGTGTTCCTCCTCCTCAAGGTTAT 70 90 110 CCACCGGAGGGATATCCAAAAGATGCTTATCCACCACAAGGATATCCTCCTCAGGGATAT 130 150 170 CCTCAGCAAGGCTATCCACCTCAGGGATATCCTCAACAAGGTTATCCTCAGCAAGGATAT 190 210 230 CCTCCACCGTACGCGCCTCAATATCCTCCACCACCGCAGCATCAGCAACAACAGAGCAGT 250 270 290 CCTGGCTTTCTAGAAGGATGTCTTGCTGCTCTGTGTTGTTGCTGTCTCTTGGATGCTTGC 310 330 350 TTCTGATTGGAGTCTCTCTCTCTCTGCATAAAGCTTCGGGATTTATTTGTAAGAGGGTTT 370 390 410 TGGTTAAACAAAAACCTTAATTGATTTGTGGGGCATTAAAAATGAATCTCTCGATGATTC 430 450 470 TCTTTCGTTTTATGTGTAATGTTCTTCGGTTCATAACATTTTAACTATTGTCTATCGACG 490 510 530 TTCTGCCTTAGTTTGTATTTGATTATGGGAATGTAAATTGGTTGGGAGACACTATTCTAT 5 550 570 GCCATAGTTTATTGCTTGGATCTTCAAAAAAAAAAAAAAAAAA SEQ ID NO: 73 Amino acid sequence of GG ArgGluThrMetSerGlnTyrAsnGlnProProValGlyValProProProGlnGlyTyr 10 20 ProProGluGlyTyrProLysAspAlaTyrProProGlnGlyTyrProProGlnGlyTyr 30 40 ProGlnGlnGlyTyrProProGlnGlyTyrProGlnGlnGlyTyrProGlnGlnGlyTyr 50 60 ProProProTyrAlaProGlnTyrProProPrσProGlnHisGlnGlnGlnGlnSerSer 70 80 ProGlyPheLeuGluGlyCysLeuAlaAlaLeuCysCysCysCysLeuLeuAspAlaCys 90 100 Phe SEQ IDNO: 74 Nucleic acid sequence of HH 10 30 50 AGTGATGTTCTTCCTAAGTCCGTTGACTGGAGAAACGAAGGCGCAGTGACTGAAGTCAAA 70 90 110 GATCAAGGCCTTTGCAGGAGTTGTTGGGCTTTCTCCACTGTGGGAGCAGTGGAAGGCTTA 130 150 170 AACAAGATTGTGACTGGAGAGCTAGTAACTTTGTCTGAGCAAGATTTGATCAATTGTAAC 190 210 230 AAAGAAAACAATGGTTGCGGAGGAGGCAAAGTCGAGACAGCCTATGAGTTCATCATGAAC 250 270 290 AATGGTGGTCTTGGTACCGACAACGATTATCCTTACAAAGCTCTCAATGGAGTCTGCGAA 310 330 350 GGCCGCCTCAAGGAAGACAACAAGAATGTTATGATTGATGGGTATGAGAATTTGCCTGCA 370 390 410 AACGATGAAGCCGCTCTCATGAAAGCGGTTGCTCACCAGCCTGTGACTGCCGTTGTCGAT 6 430 450 470 TCCAGCAGCCGAGAGTTTCAGCTTTATGAATCGGGAGTGTTTGACGGAACTTGCGGAACA 490 510 530 AACCTAAACCATGGTGTTGTTGTGGTCGGGTATGGAACCGAGAATGGTCGTGACTACTGG 550 570 590 ATTGTGAAAAACTCGAGGGGCGACACATGGGGGGAGGCTGGCTACATGAAGATGGCTCGC 610 630 650 AACATTGCCAATCCAAGAGGCATATGTGGCATCGCAATGCGAGCTTCATACCCTCTCAAG 670 690 710 AACTCGTTTTCTACGGATAAAGTTTCGGTTGCCTAATAATATGAACTAAATGTATGCCAT 730 750 770 GGAACGGATCGGTTAAGCCATTATCGTTATTCGACTTTGAAGGAAACTAAAAAATAATGT 790 810 830 GGTCGATTGGTTTGGTTTTGTTATATATTATGCATTTGTATGGGGGTCAGTCAATGTTTG 850 870 890 AACTTTGTATAATATTTCTTTGGGTCTAGTGATAAATATTTTCCCTTTTGCGAAAAAAAA 910 AAAAAAAAAA SEQ ID NO: 75 Amino acid sequence of HH SerAspValLeuProLysSerValAspTrpArgAsnGluGlyAlaValThrGluValLys 10 20 AspGlnGlyLeuCysArgSerCysTrpAlaPheSerThrValGlyAlaValGluGlyLeu 30 40 AsnLysIleValThrGlyGluLeuValThrLeuSerGluGlnAspLeuIleAsnCysAsn 50 60 LysGluAsnAsnGlyCysGlyGlyGlyLysValGluThrAlaTyrGluPhelleMetAsn 70 80 AsnGlyGlyLeuGlyThrAspAsnAspTyrProTyrLysAlaLeuAsnGlyValCysGlu 90 100 GlyArgLeuLysGluAspAsnLysAsnValMetlleAspGlyTyrGluAsnLeuProAla 110 120 AsnAspGluAlaAlaLeuMetLysAlaValAlaHisGlnProValThrAlaValValAsp 130 140 7 SerSerSerArgGluPheGlnLeuTyrGluSerGlyValPheAspGlyThrCysGlyThr 150 160 AsnLeuAsnHisGlyValValValValGlyTyrGlyThrGluAsnGlyArgAspTyrTrp 170 180 IleValLysAsnSerArgGlyAspThrTrpGlyGluAlaGlyTyrMetLysMetAlaArg 190 200 AsnlleAlaAsnProArgGlylleCysGlylleAlaMetArgAlaSerTyrProLeuLys 210 220 AsnSerPheSerThrAspLysValSerValAla 230 SEQ ID NO: 76 Nucleic acid sequence of I 10 30 50 AGCGAAATGCCAGTTTCAGCTCCATCTCCGCCTCGTCTTCATTCTCCGTTCATTCACTGT 70 90 110 CCCATCAATTTCACTCCTTCTTCTTTCTCGGCGAGGAATCTCCGGTCGCCGTCAACATCT 130 150 170 TATCCCCGAATCAAAGCTGAACTCGATCCCAACACGGTAGTCGCGATATCTGTAGGCGTA 190 210 230 GCAAGCGTCGCATTAGGAATCGGAATCCCTGTGTTCTACGAGACTCAAATCGACAATGCG 250 270 290 GCTAAGCGAGAGAATACTCAACCTTGTTTTCCCTGTAATGGCACCGGAGCTCAGAAATGC 310 330 350 AGATTGTGTGTGGGAAGTGGTAATGTGACCGTAGAGCTTGGTGGAGGAGAGAAAGAAGTC 370 390 410 TCAAACTGTATCAACTGTGATGGTGCTGGTTCCTTAACTTGCACTACTTGTCAAGGCTCT 430 450 470 GGTGTTCAACCTCGATACCTTGATCGAAGGGAGTTCAAGGACGATGACTAAATACCTTGC 490 510 530 TCTAAGGAACATTTCTTTTCTTCTCCCTTCTCACATTTCTTCATTGTACAATGCTGTTTT 550 570 590 GTTCACCAAACATGTTGAGAGAACATCATGACATGGATATTGTAATTGTGAAAGAAAACC 610 630 650 28 ACCAGAGTTCAATCAAATGTTTCTTCTTGTACTTAAAAAAAAAAAAAAAAAAA SEQ ID NO: 77 Amino acid sequence of I SerGluMetProValSerAlaProSerProProArgLeuHisSerProPhelleHisCys 10 20 ProIleAsnPheThrProSerSerPheSerAlaArgAsnLeuArgSerProSerThrSer 30 40 TyrProArglleLysAlaGluLeuAspProAsnThrValValAlalleSerValGlyVal 50 60 AlaSerValAlaLeuGlylleGlylleProValPheTyrGluThrGlnlleAspAsnAla 70 80 AlaLysArgGluAsnThrGlnProCysPheProCysAsnGlyThrGlyAlaGlnLysCys 90 100 ArgLeuCysValGlySerGlyAsnValThrValGluLeuGlyGlyGlyGluLysGluVal 110 120 SerAsnCysIleAsnCysAspGlyAlaGlySerLeuThrCysThrThrCysGlnGlySer 130 140 GlyValGlnProArgTyrLeuAspArgArgGluPheLysAspAspAsp 150 SEQ IDNO: 78 Nucleic acid sequence of II 10 30 50 AGAGAAAACATGGGAGGTGACAATGATAATGACAAAGACAAAGGGTTTCATGGGTATCCT 70 90 110 CCCGCTGGATACCCACCCCCTGGGGCTTATCCACCCGCTGGATACCCACAACAAGGTTAC 130 150 170 CCTCCACCACCCGGTGCTTACCCGCCTGCAGGTTATCCTCCGGGTGCCTACCCACCTGCT 190 210 230 CCTGGTGGTTATCCTCCCGCCCCTGGTTATGGTGGTTATCCTCCAGCTCCTGGTTATGGA 250 270 290 9 GGTTATCCTCCTGCACCTGGTCATGGTGGTTACCCTCCTGCTGGCTATCCTGCTCATCAC 310 330 350 TCAGGACACGCAGGAGGAATTGGGGGTATGATTGCAGGTGCTGCAGCTGCCTATGGAGCT 370 390 410 CACCACGTATCTCATAGCTCTCACTGTCCTTACGGACATGCTGCATATGGTCACGGTTTT 430 450 470 GGCCATGGTCATGGCTATGGCTATGGTCATGGTCATGGTAAGTTCAAGCATGGGAAGCAC 490 510 530 GGGAAGTTCAAGCATGGGAAGCATGGAATGTTTGGAGGAGGCAAGTTCAAGAAGTGGAAG 550 570 590 TGATCTAGCTATTACCTTGTGTGAATTTGTCTGGACTGACCAATGTTTCAAATAAGCCCT 610 630 650 AAACATTATATAAGTTGACTTTCGTCGGTTAGATTGCTGGTTCGAGTTGGAATAATTGAA 670 690 710 ACTTAATTAGTATCAAATCTTATTGTGTACTTTAAAGCTATCGTTGGCTTTATAATGACA 730 750 770 GATTCTGGTTTCGGTGTGTTGTTTTAAGATTTTTGTATATACTGTTTTTTACATTGCTTA 790 810 AGCTTATAGAAGTCATGATTATGATTAAAAAAAAAAAAAAAAAA SEQ ID NO: 79 Amino acid sequence of II ArgGluAsnMetGlyGlyAspAsnAspAsnAspLysAspLysGlyPheHisGlyTyrP.ro 10 20 ProAlaGlyTyrProProProGlyAlaTyrProProAlaGlyTyrProGlnGlnGlyTyr 30 40 ProProProProGlyAlaTyrProProAlaGlyTyrProProGlyAlaTyrProProAla 50 60 ProGlyGlyTyrProProAlaProGlyTyrGlyGlyTyrProProAlaProGlyTyrGly 70 80 GlyTyrProProAlaProGlyHisGlyGlyTyrProProAlaGlyTyrProAlaHisHis 90 100 SerGlyHisAlaGlyGlylleGlyGlyMetlleAlaGlyAlaAlaAlaAlaTyrGlyAla 110 120 HisHisValSerHisSerSerHisCysProTyrGlyHisAlaAlaTyrGlyHisGlyPhe 0 130 140 GlyHisGlyHisGlyTyrGlyTyrGlyHisGlyHisGlyLysPheLysHisGlyLysHis 150 160 GlyLysPheLysHisGlyLysHisGlyMetPheGlyGlyGlyLysPheLysLysTrpLys 170 180 SEQ ID NO: 80 Nucleic acid sequence of K 10 30 50 AGTGTCACTACTCCATCCGAGGAGGATTCAAACAACGGTTTACCGGTTCAGCAACCCGGT 70 90 110 ACACCGAACCAGCGAACCAGAGTTCCCGTGAGTCAATTCGCGCCGCCGAATTATCAGCAA 130 150 170 GCTAATGTTAACCTATCTGTTGGGAGGCCATGGAGCACTGGTTTGTTTGATTGTCAAGCA 190 210 230 GACCAAGCCAATGCCGTTTTGACCACAATTGTACCTTGTGTAACATTTGGACAAATAGCA 250 270 290 GAAGTGATGGATGAAGGAGAGATGACTTGTCCTCTTGGAACTTTCATGTACTTATTGATG 310 330 350 ATGCCGGCTTTATGCTCTCACTGGGTGATGGGATCAAAGTATAGAGAAAAAATGAGGAGA 370 390 410 AAATTTAATCTTGTGGAAGCTCCATATTCAGATTGTGCCAGTCATGTCCTATGCCCTTGT 430 450 470 TGCTCTCTTTGTCAAGAATACAGAGAGCTCAAGATTAGGAATCTTGATCCTTCTCTAGGT 490 510 530 TGGAATGGGATACTTGCTCAAGGACAAGGACAATATGAGAGAGAAGCACCAAGTTTTGCT 550 570 590 CCTACAAATCAATATATGTCTAAGTAAACATTTGATTTTAGTTGACTTCCATATTTATTA 610 630 650 AAACATTATTTGTGGACCATTGTACAATGAAAGTGTGCTATATTAAAATTTGCAATGCAA 670 690 GTGTGAGATTGATAAAAAAAAAAAAAAAAAAA SEQ ID NO: 81 1 Amino acid sequence of K SerValThrThrProSerGluGluAspSerAsnAsnGlyLeuProValGlnGlnProGly 10 20 ThrProAsnGlnArgThrArgValProValSerGlnPheAlaProProAsnTyrGlnGln 30 40 AlaAsnValAsnLeuSerValGlyArgProTrpSerThrGlyLeuPheAspCysGlnAla 50 60 AspGlnAlaAsnAlaValLeuThrThrlleValProCysValThrPheGlyGlnlleAla 70 80 GluValMetAspGluGlyGluMetThrCysProLeuGlyThrPheMetTyrLeuLeuMet 90 100 MetProAlaLeuCysSerHisTrpValMetGlySerLysTyrArgGluLysMetArgArg 110 120 LysPheAsnLeuValGluAlaProTyrSerAspCysAlaSerHisValLeuCysProCys 130 140 CysSerLeuCysGlnGluTyrArgGluLeuLysIleArgAsnLeuAspProSerLeuGly 150 160 TrpAsnGlylleLeuAlaGlnGlyGlnGlyGlnTyrGluArgGluAlaProSerPheAla 170 180 ProThrAsnGlnTyrMetSerLys SEQ ID NO: 82 Nucleic acid sequence of M 10 30 50 AGAAAATACGAAAAGGTCTCCCTCCCAGCACCTTACGTGGCTGGACACTCGAGCCATCAC 70 90 110 GAAGACGACGGTCAATACTATCCCGGCAAATACGAAAAAGCCTCCCTCCCAGCACCTTAC 130 150 170 GTGGCCGGATATCCGAGCCATCATGAAGACGATGGTCAATACTATCCTGGCAAATACGAA 190 210 230 AAGGTCTCCCTCCCAGCACCTTACGTGGTCGGACACCCGAGCCACTCCGAAGATGATGGC 250 270 290 CAATACTATCCCGGCAAATACGAAAAGGCCTCCGTCCCATCAGCTTACGTGGCCGAACAC 310 330 350 TCGAGCCACTCCGAAGATGATGGCCAATACTATCCTGGCAAATACGAAAAGCCCGAACAC 2 370 390 410 CATTACTGAAAACTCTCACACAACAATGATTCTCATCCTTCCGTAGTCTTTTAATTCGAC 430 450 470 TTTTAACAATAAAAACGTGATCTTAATTTTTCATCAAAAAAAAAAAAAAAAAAA SEQ ID NO: 83 Amino acid sequence of M ArgLysTyrGluLysValSerLeuProAlaProTyrValAlaGlyHisSerSerHisHis 10 20 GluAspAspGlyGlnTyrTyrProGlyLysTyrGluLysAlaSerLeuProAlaProTyr 30 40 ValAlaGlyTyrProSerHisHisGluAspAspGlyGlnTyrTyrProGlyLysTyrGlu 50 60 LysValSerLeuProAlaProTyrValValGlyHisProSerHisSerGluAspAspGly 70 80 GlnTyrTyrProGlyLysTyrGluLysAlaSerValProSerAlaTyrValAlaGluHis 90 100 SerSerHisSerGluAspAspGlyGlnTyrTyrProGlyLysTyrGluLysProGluHis 110 120 HisTyr SEQ ID NO: 84 Nucleic acid sequence of 00 10 30 50 AGCCGATCTCAGATTCTTCCATCTTCCAGGAGGAATTTCAGTGTGGCGACCACACAGCTT 70 90 110 GGCATTCCAACAGACGATCTAGTCGGCAATCACACCGCCAAATGGATGCAGGATAGAAGC 130 150 170 AAGAAATCACCTATGGAACTGATTAGTGAGGTTCCACCTATCAAAGTTGATGGAAGGATT 190 210 230 GTTGCTTGTGAAGGAGACACCAATCCGGCCCTAGGTCATCCAATCGAGTTCATATGCCTC 3 250 270 290 GACCTAAATGAGCCTGCGATCTGCAAGTACTGCGGCCTTCGTTATGTTCAAGATCATCAC 310 330 350 CATTGAGGCAAATTCTGAAAGTGAACTGCTGGTCTCTCTCCCCTTTTTATTGCATTTTTA 370 390 410 AGTTTGTGTATTGTTTTTTTCTGGTGTGCCTACTACATCTTCAGCTATATTATCTAATAA 430 450 470 AGGATTCGATCAAAGTCGGGTAAGTTTGATTTTTGTTTGATCTCACTTCAGCACTTGTCA 490 510 530 TGTTGTAACATTCAATCTCTGATATCACTGTCTTTTACATGCCAAAAAAAAAAAAAAAAA 550 AAAAAAAAAAAAAAAA SEQ ID NO: 85 Amino acid sequence of OO SerArgSerGlnlleLeuProSerSerArgArgAsnPheSerValAlaThrThrGlnLeu 10 20 GlylleProThrAspAspLeuValGlyAsnHisThrAlaLysTrpMetGlnAspArgSer 30 40 LysLysSerProMetGluLeuIleSerGluValProProlleLysValAspGlyArglle 50 60 ValAlaCysGluGlyAspThrAsnProAlaLeuGlyHisProIleGluPhelleCysLeu 70 80 AspLeuAsnGluProAlalleCysLysTyrCysGlyLeuArgTyrValGlnAspHisHis 90 100 HisEndGlyLysPhe SEQ ID NO: 86 Nucleic acid sequence of P 10 30 50 AGAACAGCTCGAGTTCCTTATGGGCCTAGACTCTCTGGTGGTGGTTACAACCGATCTGGA 70 90 110 AACAGGGTTCCGCGTAACAAACCAAGCTTCCCCAATAGCACCGAGTCCAATGGTGAGGCT 4 130 150 170 AATCAATTCAATGGCCCAAGAATAATGAACCCCCATGCTGCTGAGTTCATACCGAGTCAA 190 210 230 CCTTGGGTTTCTAATGGGTATCCAGTGTCACCAAATGGCTATTTAGCATCCCCAAATGGT 250 270 290 GCAGAAATAACACAGAATGGGTACCCTTTGTCACCAGTAGCAGGTGGATATCCGTGTAAC 310 330 350 ATGTCCGTTACACAGCCTCAGGATGGACTTGTTTCAGAGGAATTACCTGGTGCTGGAAGC 370 390 410 TCTGAGGAGAAGAGCGGAAGCGAAGAAGAAAGCAACAACGACAAAAATGCTGGAGAGGAT 430 450 470 GACGAAGCCGTTGGACAAGAAACTACAGATACACCTGAAAATGGACATTCGACAGTAGGT 490 510 530 GAAGTGGAAACCACATCACATGAGACTTGTGATGAGAAAAATGGAGAACGACAAGGAGGC 550 570 590 AAGTGCTGGGGAGATTACAGCGATAATGAAATCGAGCAAATTGAAGTTACAAGTTGAAGA 610 630 650 CGCAACTGTCTGTTACTGAAGTATTAACATTGAGGCTAAAGGAATGCGGAGACATTTTGG 670 690 710 CTCCATTGATGAGGTTAAAGGTAAACAATCATCATAGTCGAGAAAAGCATTTTTACATGT 730 750 770 GAATGTTTTGTGTTGTAGCGCAGGACCAAGGCTCGTCACTCCTGCTTTAACAACTTTTCT 790 810 830 CCTGCTTTCAGTTTTTGGTTTCATAGCTGAAAACTAGATATATTCAACTCCTTAATAAAA 850 870 GATTTGTCCCTTTGTTTAAAAAAAAAAAAAAAAAAAAAA SEQ ID NO: 87 Amino acid sequence of P ArgThrAlaArgValProTyrGlyProArgLeuSerGlyGlyGlyTyrAsnArgSerGly 10 20 AsnArgValProArgAsnLysProSerPheProAsnSerThrGluSerAsnGlyGluAla 30 40 AsnGlnPheAsnGlyProArglleMetAsnProHisAlaAlaGluPhelleProSerGln 50 60 ProTrpValSerAsnGlyTyrProValSerProAsnGlyTyrLeuAlaSerProAsnGly 5 70 80 AlaGluIleThrGlnAsnGlyTyrProLeuSerProValAlaGlyGlyTyrProCysAsn 90 100 MetSerValThrGlnProGlnAspGlyLeuValSerGluGluLeuProGlyAlaGlySer 110 120 SerGluGluLysSerGlySerGluGluGluSerAsnAsnAspLysAsnAlaGlyGluAsp 130 140 AspGluAlaValGlyGlnGluThrThrAspThrProGluAsnGlyHisSerThrValGly 150 160 GluValGluThrThrSerHisGluThrCysAspGluLysAsnGlyGluArgGlnGlyGly 170 180 LysCysTrpGlyAspTyrSerAspAsnGluIleGluGlnlleGluValThrSer 190 SEQ ID NO: 88 Nucleic acid sequence of T 10 30 50 AGAGACCATCCAGCTTACCATCAGATCCACCAGCAACAACAACAACAGCTCACTCAACAG 70 90 110 CTTCAATCTTTCTGGGAGACTCAATTCAAAGAGATTGAGAAAACCACTGATTTCAAGAAC 130 150 170 CATAGCCTTCCATTGGCAAGAATCAAGAAAATCATGAAAGCTGATGAAGATGTGCGTATG 190 210 230 ATCTCGGCCGAGGCGCCTGTTGTGTTCGCCAGGGCCTGCGAGATGTTTATTCTGGAGCTT 250 270 290 ACGTTAAGGTCTTGGAACCATACTGAGGAGAACAAGAGAAGGACGTTGCAGAAGAATGAT 310 330 350 ATCGCGGCTGCGGTGACTAGAACTGATATTTTTGATTTTCTTGTGGATATTGTTCCTCGG 370 390 410 GAGGATCTTCGTGATGAAGTCTTGGGTGGTGTTGGTGCTGAAGCTGCTACAGCTGCGGGT 430 450 470 TATCCGTATGGATACTTGCCTCCTGGAACAGCTCCAATTGGGAACCCGGGAATGGTTATG 490 510 530 GGTAACCCGGGCGCGTATCCGCCGAACCCGTATATGGGTCAGCCAATGTGGCAACAACCA 550 570 590 GGACCTGAGCAGCAGGATCCTGACAATTAGCTTGGCCTAATAAACTAGCCGTCTAATTCG 6 610 630 650 AAGCTCTCCCCGGTGGATCTACTCAAGAAGAAGAATGTTAATAGAAAACTATTGCGACAT 670 690 710 AAAAAGTTTGGTGTAGTAGAATAATTTCTGTTTTATGATCCATGGATTTATCTATTGTTA 730 750 770 TTCAGTTTGGTTTATCTTGTCATCAAACTGTTTTCGGTCAATGTAACAAATTCATAAACT 790 810 830 GAGAATTGAACTTACAAAAGGCTAGATTACTACTTATAAAGTTCAAAGCTAAAAAAAAAA AAAAAAAA SEQ ID NO: 89 Amino acid sequence of T ArgAspHisProAlaTyrHisGlnlleHisGlnGlnGlnGlnGlnGlnLeuThrGlnGln 10 20 LeuGlnSerPheTrpGluThrGlnPheLysGluIleGluLysThrThrAspPheLysAsn 30 40 HisSerLeuProLeuAlaArglleLysLysIleMetLysAlaAspGluAspValArgMet 50 60 IleSerAlaGluAlaProValValPheAlaArgAlaCysGluMetPhelleLeuGluLeu 70 80 ThrLeuArgSerTrpAsnHisThrGluGluAsnLysArgArgThrLeuGlnLysAsnAsp 90 100 IleAlaAlaAlaValThrArgThrAspIlePheAspPheLeuValAspIleValProArg 110 120 GluAspLeuArgAspGluValLeuGlyGlyValGlyAlaGluAlaAlaThrAlaAlaGly 130 140 TyrProTyrGlyTyrLeuProProGlyThrAlaProIleGlyAsnProGlyMetValMet 150 160 GlyAsnProGlyAlaTyrProProAsnProTyrMetGlyGlnProMetTrpGlnGlnPro 170 180 GlyProGluGlnGlnAspProAspAsn 37 SEQ ID NO: 90 Nucleic acid sequence of X 10 30 50 AGATTCGCTATTCCTGGCAAAGAAAGACAAGATTCTGTTTACAGTGGACTTCAGGAAATC 70 90 110 GATGTGAACTCTGAGCTTGTTTGTATCCACGACTCTGCCCGACCATTGGTGAATACTGAA 130 150 170 GATGTCGAGAAGGTCCTTAAAGATGGTTCCGCGGTTGGAGCAGCTGTACTTGGTGTTCCT 190 210 230 GCTAAAGCTACAATCAAAGAGGTCAATTCTGATTCGCTTGTGGTGAAAACTCTCGACAGA 250 270 290 AAAACCCTATGGGAAATGCAGACACCACAGGTGATCAAACCAGAGCTATTGAAAAAGGGT 310 330 350 TTCGAGCTTGTAAAAAGTGAAGGTCTAGAGGTAACAGATGACGTTTCGATTGTTGAATAC 370 390 410 CTCAAGCATCCAGTTTATGTCTCTCAAGGATCTTATACAAACATCAAGGTTACAACACCT 430 450 470 GATGATTTACTGCTTGCTGAGAGAATCTTGAGCGAGGACTCATGAGATATTATATCATTT 490 510 530 ACTTAGTAAGAAGACGTGTCAAGGGTATGCATGAAAAATGTTTTATTGAAATCTTTGCAT 550 570 590 CCTAGTTTGGTGGTTTATAAAATGTGCAAGATAATTGTTTCACTGAAAACTACTTGCTGT 610 630 650 GAATATGGATTCGAACAGAGCCAATTCGAAGTAGAATTTGCATATTGTAAAAAAAAAAAA 670 AAAAAAAAAA SEQ ID NO: 91 Amino acid sequence of X ArgPheAlalleProGlyLysGluArgGlnAspSerValTyrSerGlyLeuGlnGluIle 10 20 AspValAsnSerGluLeuValCysIleHisAspSerAlaArgProLeuValAsnThrGlu 30 40 AspValGluLysValLeuLysAspGlySerAlaValGlyAlaAlaValLeuGlyValPro 50 60 AlaLysAlaThrlleLysGluValAsnSerAspSerLeuValValLysThrLeuAspArg 70 80 LysThrLeuTrpGluMetGlnThrProGlnVallleLysProGluLeuLeuLysLysGly 90 100 PheGluLeuValLysSerGluGlyLeuGluValThrAspAspValSerlleValGluTyr 110 120 LeuLysHisProValTyrValSerGlnGlySerTyrThrAsnlleLysValThrThrPro 130 140 AspAspLeuLeuLeuAlaGluArglleLeuSerGluAspSer 150

Claims: THE CLAIMS What is Claimed Is: 1. An isolated DNA sequence that encodes a LSDl polypeptide. 2. The isolated DNA sequence of claim 1, wherein the sequence is selected from the group consisting of SEQ ID NO13, SEQ ID NO 14 and SEQ ID NO 15. 3. The isolated DNA sequence of claim 1, wherein the sequence comprises SEQ ID NO 13. 4. The isolated DNA sequence of claim 1 , wherein the sequence comprises SEQ ID NO 14. 5. The isolated DNA sequence of claim 1, wherein the sequence comprises SEQ ID NO 15. 6. The isolated DNA sequence of claim 1 , wherein the DNA is cDNA. 7. The isolated DNA sequence of claim 1 , wherein the DNA is genomic. 8. The isolated DNA sequence of claim 1 , wherein the polypeptide comprises SEQ ID NO 16. 9. The isolated DNA sequence of claim 1 , wherein the polypeptide comprises SEQ ID NO 17. 10. A protein encoded by the isolated DNA sequence of claim 1. 11. A chimeric construction comprising a promoter sequence and a DNA sequence according to claim 1. 12. A transformation vector comprising the isolated DNA sequence of claim 1. 13. A mutated DNA sequence derived from the DNA sequence of claim 1. 14. A transgenic plant expressing LSDl mutant genes that affect resistance to herbicidal compounds that normally result in plant cell death. 15. A transgenic plant expressing LSDl mutant genes which affect resistance to plant pathogens that normally result in plant cell death. 16. A messenger RNA encoding LSD 1. 17. An isolated DNA sequence that encodes the zinc finger consensus selected from the group consisting of SEQ ID NOS 1-3. 18. A protein containing a zinc fmger protein selected from the group consisting of CxxCxRxxLMYxxGASxVxCxxC, CxxCRxxLMYxxGASxRxVxCxxC, CxxCxxLLMYxxGAxSxCxxC, CxxCxxLLxYxxGxxxVxCSSC, CSGCRNLLMYPVGATSVCCAVC, CGGCHTLIMYIRGATSVQCSCC, CGNCMMLLMYQYGARSVKCAVC, CGSCRRLLSYLRGSKHVKCSSC, and CNNCKLLLMYPYGAPAVRCSSC, wherein x is any substituted amino acid. 19. A gene encoding a zinc fmger protein according to claim 18. 20. An isolated DNA sequence encoding a protein according to claim 18. 21. A recombinant plant transformed with the DNA sequence as claimed in claim 1. 22. A recombinant plant transformed with the DNA sequence as claimed in claim 20. 23. An isolated DNA molecule that hybridizes under hybridization conditions to a DNA sequence as claimed in claim 1. 24. An isolated DNA molecule that hybridizes under hybridization conditions to a DNA sequence as claimed in claim 20. 25. An isolated DNA sequence that encodes a LSDl homologue. 26. The isolated DNA sequence of claim 25, wherein the homologue is selected from the group consisting of LOLl and LOL2. 27. The isolated DNA sequence of claim 25, wherein the homologue is selected from the group consisting of SEQ ID NO:48, SEQ ID NO:55, SEQ ID NO:60 and SEQ ID NO:62. 28. The isolated DNA sequence of claim 25, wherein the sequence is selected from the group consisting of SEQ ID NO:47, SEQ ID NO:54, and SEQ ID NO:59. 29. The isolated DNA sequence of claim 25, wherein the sequence comprises SEQ ID NO 47. 30. The isolated DNA sequence of claim 25, wherein the sequence comprises SEQ ID NO 54. 31. The isolated DNA sequence of claim 25, wherein the sequence comprises SEQ ID NO 59. 32. The isolated DNA sequence of claim 25, wherein the DNA is cDNA. 33. The isolated DNA sequence of claim 25, wherein the DNA is genomic. 34. A recombinant plant transformed with the DNA sequence as claimed in claim 25. 35. An isolated DNA molecule that hybridizes under hybridization conditions to a DNA sequence as claimed in claim 25. 36. A protein encoded by the isolated DNA sequence of claim 25. 37. A chimeric construction comprising a promoter sequence and a DNA sequence according to claim 25. 38. A transformation vector comprising the isolated DNA sequence of claim 25. 39. A mutated DNA sequence derived from the DNA sequence of claim 25. 40. A transgenic plant expressing LOLl mutant genes that affect resistance to herbicidal compounds that normally result in plant cell death. 41. A transgenic plant expressing LOLl mutant genes which affect resistance to plant pathogens that normally result in plant cell death. 42. A messenger RNA encoding LOLl . 43. A transgenic plant expressing LOLl mutant genes that affect resistance to herbicidal compounds that normally result in plant cell death. 44. A transgenic plant expressing LOLl mutant genes which affect resistance to plant pathogens that normally result in plant cell death. 45. A messenger RNA encoding LOL2. 46. A nucleic acid that interacts with LSDl, selected from the group consisting of the nucleic acid sequences set forth in SEQ ID NOS:66-91. 47. A protein encoded by a nucleic acid according to claim 46.

Inventors: DANGL JEFFERY L, DIETRICH ROBERT A, EPPLE PETRA M, RICHBERG MICHAEL H, DANGL, JEFFERY, L., DIETRICH, ROBERT, A., EPPLE, PETRA, M., RICHBERG, MICHAEL, H.
Applicants: DANGL JEFFERY L, DIETRICH ROBERT A, EPPLE PETRA M, RICHBERG MICHAEL H, UNIV NORTH CAROLINA, DANGL, JEFFERY, L., DIETRICH, ROBERT, A., EPPLE, PETRA, M., RICHBERG, MICHAEL, H., THE UNIVERSITY OF NORTH CAROLINA AT CHAPEL HILL
Application year: 1998
Main classification: A01H5
IPC codes: C07K14, C12N15