PRODUCTION OF APOMICTIC SEED

Abstract: The present invention provides, inter alia, a method of producing apomictic seeds comprising the steps of: (i) transforming plant material with a nucleotide sequence encoding a protein the presence of which in a cell, or membrane thereof, renders said cell embryogenic, (ii) regenerating the thus transformed material into plants, or carpel containing parts thereof, and (iii) expressing the sequence in the vicinity of the embryo sac. The protein may be a leucine repeat rich receptor kinase which preferably is modified to the extent that the ligand binding domain is deleted or functionally inactivated.

Description: Production of Apomictic Seed The present invention relates to the production of genetically transformed plants. In particular the invention relates inter alia to a process for inducing apomixis, to the apomictic seeds which result from the process, and to the plants and progeny thereof which result from the germination of such seeds. Apomixis, which is vegetative (non-sexual) reproduction through seeds, is a genetically controlled reproductive mechanism found in some polyploid non-cultivated species. The process is classified as gametophytic or non-gametophytic. In gametophytic apomixis - of which there are two types (apospory and diplospory), multiple embryo sacs which typically lack antipodal nuclei are formed, or else megasporogenesis in the embryo sac takes place. In adventitious embryoπy (non-gametophytic apomixis), a somatic embryo develops directly from the cells of the embryo sac, ovary wall or integuments. In adventitious embryony, somatic embryos from surrounding cells invade the sexual ovary, one of the somatic embryos out-competes the other somatic embryos and the sexual embryo and utilizes the produced endosperm. Were apomixis to be a controllable and reproducible phenomenon it would provide many advantages in plant improvement and cultivar development in the case that sexual plants are available as crosses with the apomictic plant. For example, apomixis would provide for true-breeding, seed propagated hybrids. Moreover, apomixis could shorten and simplify the breeding process so that setting and progeny testing to produce and/or stabilize a desirable gene combination could be eliminated. Apomixis would provide for the use as cultivars of genotypes with unique gene combinations since apomictic genotypes breed true irrespective of heterozygosity. Genes or groups of genes could thus be "pyramided and "fixed" in super genotypes. Every superior apomictic genotype from a sexual- apomict j c cross would have the potential to be a cultivar. Apomixis would allow plant breeders to develop cultivars with specific stable traits for such characters as height, seed and forage quality and maturity. Breeders would not be limited in their commercial production of hybrids by (i) a cytoplasmic-nuclear interaction to produce male sterile female parents or (ii) the fertility restoring capacity of a pollinator. Almost all cross-compatible germplasm could be a potential parent to produce apomictic hybrids. Finally, apomixis would simplify commercial hybrid seed production. In particular, (i) the need for physical isolation of commercial hybrid production fields would be eliminated; (ii) all available land could be used to increase hybrid seed instead of dividing space between pollinators and male sterile lines; and (iii) the need to maintain parental line seed stocks would be eliminated. The potential benefits to accrue from the production of seed via apomixis are presently unrealized, to a large extent because of the problem of engineering apomictic capacity into plants of interest. The present invention provides a solution to that problem in that it provides the means for obtaining plants which exhibit the adventitious embryony type of apomixis. According to the present invention there is provided a method of producing apomictic seeds comprising the steps of: (i) transforming plant material with a nucleotide sequence encoding a protein the presence of which in an active form in a cell, or membrane thereof, renders said cell embryogenic, (ii) regenerating the thus transformed material into plants, or carpel-containing parts thereof, and (iii) expressing the sequence in the vicinity of the embryo sac. By "vicinity of the embryo sac" is meant in one or more of the following: carpel, integuments, ovuie, ovule premordium, ovary wall, chalaza, nucellus, funicle and placenta. The skilled man will recognize that the term "integuments" also includes those tissues, such as endothelium, which are derived therefrom. By "embryogenic" is meant the capability of cells to develop into an embryo under permissive conditions. It will be appreciated that the term "in an active form" includes proteins which are truncated or otherwise mutated with the proviso that they initiate or amplify embryogenesis whether or not in doing this they interact with the signal transduction components that they otherwise would in the tissues in which they are normally present The term "plant material" includes protoplasts, isolated plant cells (such as stomatal guard cells) possessing a cell wall, pollen, whole tissues such as emerged radicle, stem, leaf, petal, hypocotyl section, apical meristem, ovaries, zygotic embryo per se, roots, vascular bundle, pericycle, anther filament, somatic embryos and the like. A further embodiment of the invention relates to a DNA molecule comprising a nucleotide sequence encoding a protein the presence of which in an active form in a cell, or membrane thereof, renders said cell embryogenic. The said nucleotide sequence may be introduced into the plant material, inter alia, via a bacterial or viral vector, by micro-injection, by co-incubation of the plant material and sequence in the presence of a high molecular weight glycol or by coating of the sequence onto the surface of a biologically inert particle which is then introduced into the material. Expression of the sequence may yield a protein kinase capable of spanning a plant cell membrane. Typically the kinase may be a leucine rich repeat receptor like kinase which has the capacity to auto-phosphorylate. The skilled man will recognize what is meant by the term "leucine rich repeat receptor like kinase". Examples of such proteins include Arabidopsis RLK5 (Walker, 1993), Arabidopsis RPS2 (Bent et al. 1994), Tomato CF-9 gene product (Jones ef al. 1994), Tomato N (Whitham et al. 1994), Petunia PRK1 (Mu er al. 1994), the product of the Dmsophila Toll gene (Hashimoto ef al. 1988), the protein kinase encoded by the rice OsPKIO gene (Zhao et al. 1994), the translation product of the rice EST clone ric2976 and the product of the Dnosophila Pelle gene (Shelton and Wasserman, 1993). Still further examples of such proteins include the TMK1 , Clavatal, Erecta, and TMKL1 gene products from Arabidopsis, the Flightless-1 gene product from Dmsophila, the TrkC gene product from pig, the rat LhCG receptor and FSH receptor, the dog TSH receptor, and the human Trk receptor kinase. The protein may comprise a ligand binding domain, a proline box, a transmembrane domain, a kinase domain and a protein binding domain. In many receptor kinases the extracellular (ligand binding) domain serves as an inhibitor of the kinase domain in the ligand-f ree state. This arrest is removed after binding of the ligand. Accordingly, in one embodiment of the invention the protein either lacks a ligand binding domain or the domain is functionally inactivated so that the kinase domain can be constftutiveiy active in the absence of an activating signal (ligand). Whether or not the protein possesses a ligand binding domain - functional or otherwise, once expressed and incoφorated into the plant cell membrane the protein binding domain is preferably located intra-cellulariy. In a preferred embodiment of the method, the said sequence further encodes a cell membrane targeting sequence. The sequence may be that which is depicted in SEQ ID Nos. 1 , 2, 20, or 32, or it may be similar in that it is complementary to a sequence which hybridizes under stringent conditions with the said sequences and which encodes a membrane bound protein having kinase activity. By "similar" is meant a sequence which is complementary to a test sequence which is capable of hybridizing to the inventive sequence. When the test and inventive sequences are double stranded the nucleic acid constituting the test sequence preferably has a TM within 20°C of that of the inventive sequence. In the case that the test and inventive sequences are mixed together and denatured simultaneously, the TM values of the sequences are preferably within 10°C of each other. More preferably the hybridization is performed under stringent conditions, with either the test or inventive DNA preferably being supported. Thus either a denatured test or inventive sequence is preferably first bound to a support and hybridization is effected for a specified period of time at a temperature of between 50 and 70°C in double strength citrate buffered saline (SSC) containing 0.1%SDS followed by rinsing of the support at the same temperature but with a buffer having a reduced SSC concentration. Depending upon the degree of stringency required, and thus the degree of similarity of the sequences, at a particular temperature, - such as 60°C, for example - such reduced concentration buffers are typically single strength SSC containing 0.1%SDS, half strength SSC containing 0.1%SDS and one tenth strength SSC containing 0.1%SDS. Sequences having the greatest degree of similarity are those the hybridization of which is least affected by washing in buffers of reduced concentration. It is most preferred that the test and inventive sequences are so similar that the hybridization between them is substantially unaffected by washing or incubation in one tenth strength sodium citrate buffer containing 0.1%SDS. Accordingly, further comprised by the present invention is a DNA sequence as depicted in SEQ ID NOS: 22, 24, 26, 28 and 30 or a sequence which is complementary to one which hybridizes under stringent conditions with the said sequences and which encodes a membrane bound protein having kinase activity. The sequence may be modified in that known mRNA instability motifs or polyadenylation signals may be removed and/or codons which are preferred by the plant into which the sequence is to be inserted may be used so that expression of the thus modified sequence in the said plant may yield substantially similar protein to that obtained by expression of the unmodified sequence in the organism in which the protein is endogenous. ln order to obtain expression of the sequence in the regenerated plant (and in particular the carpel thereof) in a tissue specific manner the sequence is preferably under expression control of an inducible or developmentally regulated promoter, typically one of the following: a promoter which regulates expression of SERK genes in planta, the Arabidopsis ANT gene promoter, the promoter of the 0126 gene from Phalaenopsis, the carrot chitinase DcEP3-1 gene promoter, the Arabidopsis AtChitlV gene promoter, the Arabidopsis LTP-1 gene promoter, the Arabidopsis bel- 1 gene promoter, the petunia fbp-7 gene promoter, the Arabidopsis AtDMCI promoter, the pTA7001 inducible promoter. The DcEP3-1 gene is expressed transiently during inner integument degradation and later in cells that line the inner part of the developing endosperm. The AtChilV gene is transiently expressed in the micropylar endosperm up to cellularisation. The LTP-1 promoter is active in the epidermis of the developing nucellus, both integuments, seed coat and early embryo. The bel-1 gene is expressed in the developing inner integument and the fbb-7 promoter is active during embryo sac development. The Arabidopsis ANT gene is expressed during integument development, and the 0126 gene from Phalaenopsis is expressed in the mature ovule. It is most preferred that the sequence is expressed in the somatic cells of the embryo sac, ovary wall, nucellus, or integuments. The endosperm within the apomictic seed results from fusion of polar nuclei within the embryo sac with a pollen-derived male gamete nucleus. It is preferred that the sequence encoding the protein is expressed prior to fusion of the polar nuclei with the male gamete nucleus. The invention further includes a DNA, but preferably a recombinant DNA, comprising a sequence encoding a protein the presence of which in an active form in a cell, or membrane thereof, renders said cell embryogenic. Preferred is a DNA encoding a protein which is a leucine rich repeat receptor like kinase and comprises a ligand binding domain, a proline box, a transmembrane domain, a kinase domain and a protein binding domain, the ligand binding domain optionally being absent or functionally inactive. In particular, the invention embodies a DNA comprising a DNA sequence encoding a N-terminal protein fragment having the following amino acid sequence: Gh Ser Trp Asp Pro Thr Leu Val Asn Pro Cys ThrTrp Phe HE Val Thr Cys Asn. A specific embodiment of the invention relates to a DNA comprising a DNA sequence encoding a protein having the sequence depicted in SEQ ID Nos. 3 or 21 , or a protein substantially similar thereto which is capable of being membrane bound and which has kinase activity. By substantially similar is meant a pure protein having an amino acid sequence which is at least 90% similar to the sequence of the proteins depicted in SEQ ID No 3 below. In the context of the present invention, two amino acid sequences with at least 90% similarity to each other have at least 90% identical or conservatively replaced amino acid residues in a like position when aligned optimally allowing for up to 8 gaps with the pmviso that in respect of each gap a total not more than 4 amino acid residues is affected. For the purpose of the present invention conservative replacements may be made between amino acids within the following groups: (i) Serine and Threonine; (ii) Glutamic acid and Aspartic acid; (iii) Arginine and Lysine; (iv) Asparagine and Glutamine; (v) Isoleucine, Leucine, Valine and Methionine; (vi) Phenylalanine, Tyrosine and Tryptophan (vii) Alanine and Glycine In addition, non-conservative replacements may also occur at a low frequency. Accordingly, the invention futher embodies a DNA compπsing a DNA sequence encoding a N-terminal protein fragment having the following amino acid sequence: Val Xaa Gh Ser Trp Asp ProThrLeu Val Asn Pro CysThrTrp Phe His Val ThrCys Asn, with Xaa being a variable amhoacti,bLit preferably LeuorVai Especially preferred within the scope of the invention is a DNA comprising a DNA sequence encoding a N-terminal protein fragment having the following amino acid sequence: Val Xaa Gh Ser Trp Asp Pro Thr Leu Val Asn Pro Cys Thr Trp Phe He Val Thr Cys Asn XabXac XadXaeVaJXafArgVal Aφ Leu GVAsn Xag Xah Leu SerGry te Ljeu Xa FtoGkj Le^ Xaa to Xak representing variable amino acids, but preferably Xaa = Leu or Val Xab=AsnorGh Xac = Glu or Asp or Hε Xad= AsnorHs Xae = Ser or Arg or Gh Xaf = He or Thr Xag=AtaorSer Xah=GJuorAsn Xai=ValorAla Xaj=ValorLys Xak=LysorGlu Xal=AsnorHs It is preferred that the DNA further encodes a cell membrane targeting sequence, and that the protein encoding region is under expression control of a developmentally regulated or inducible promoter, such as, for example, a promoter which regulates expression of SERK genes in planta, the carrot chitinase DcEP3-1 gene promoter, the Arabidopsis AtChitlV gene promoter, the Arabidopsis LTP-1 gene promoter, the Arabidopsis bel-1 gene promoter, the petunia fbp-7 gene promoter, the Arabidopsis ANT gene promoter, or the promoter of the 0126 gene from Phalaenopsis; the Arabidopsis AtDMCI promoter, or the pTA7001 inducible promoter. Particularly preferred embodiments of the said DNA include those depicted in SEQ ID Nos. 1 , 2, 20 or 32, or those which are complementary to one which hybridizes under stπngent conditions with the said sequences and which encode a membrane bound protein having kinase activity. As indicated above, the DNA may be modified in that known mRNA instability motifs or polyadenylation signals may be removed and/or codons which are preferred by the plant into which the DNA is to be inserted may be used so that expression of the thus modified DNA in the said plant may yield substantially similar protein to that obtained by expression of the unmodified DNA in the organism in which the protein is endogenous. The invention still further includes a vector which contains DNA as indicated in the three immediately preceding paragraphs, plants transformed with the recombinant DNA or vector, and the progeny of such plants which contain the DNA stably incoφorated, and/or the apomictic seeds of such plants or such progeny. The recombinant DNA molecules of the invention can be introduced into the plant cell in a number of art-recognized ways. Those skilled in the art will appreciate that the choice of method might depend on the type of plant, i.e. monocot or dicot, targeted for transformation. Suitable methods of transforming plant cells include microinjection (Crossway et al., BioTechniques 4:320-334 (1986)), electroporation (Riggs et al, Pmc. Natl. Acad. Sci. USA 83:5602-5606 (1986), Agmbacterium mediated transformation (Hinchee et al., Biotechnology 6:915-921 (1988)), direct gene transfer (Paszkowski et al., EMBO J. 3:2717-2722 (1984)), ballistic particle acceleration using devices available from Agracetus, Inc., Madison, Wisconsin and Dupont, Inc., Wilmington, Delaware (see, for example, Sanford et al., U.S. Patent 4,945,050; and McCabe et al., Biotechnology 6:923-926 (1988)), and protoplast transformation/regeneration methods (see U.S. Patent No. 5,350,689 issued Sept. 27, 1994 to Ciba-Geigy Coφ.). Also see, Weissinger er al., Annual Rev. Genet. 22:421-477 (1988); Sanford et al., Particulate Science and Technology 5:27-37 (1987)(onion); Christou et al., Plant Physiol. 57:671-674 (1988)(soybean); McCabe et al., Bio/Technology 6:923-926 (1988)(soybean); Datta et at., Bio/Technology 8:736-740 (1990)(rice); Klein et al., Pmc. Natl. Acad. Sci. USA, 85:4305-4309 (1988)(maize); Klein et al., Bio/Technology 6:559-563 (1988)(maize); Klein et al., Plant Physiol. 97:440-444 (1988)(maize); Fromm et al., Bio/Technology 8:833-839 (1990); and Gordon -Kamm et al., Plant Cell 2:603-618 (1990)(maize). Comprised within the scope of the present invention are transgenic plants, in particular transgenic fertile plants transformed by means of the aforedescribed processes and their asexual and/or sexual progeny, which still contain the DNA stably incoφorated, and/or the apomictic seeds of such plants or such progeny. The transgenic plant according to the invention may be a dicotyledonous or a monocotyledonous plant. Such plants include field crops, vegetables and fruits including tomato, pepper, melon, lettuce, cauliflower, broccoli, cabbage, brussels sprout, sugar beet, com, sweetcorn, onion, carrot, leek, cucumber, tobacco, alfalfa, aubergine, beet, broad bean, celery, chicory, cow pea, endive, gourd, groundnut, papaya, pea, peanut, pineapple, potato, safflower, snap bean, soybean, spinach, squashes, sunflower, sorghum, water-melon, and the like; and ornamental crops including Impatiens, Begonia, Petunia, Pelargonium, Viola, Cyclamen, VeΦena, Vinca, Tagetes, Primula, Saint Paulia, Ageratum, Amaranthus, Anthirrhinum, Aquilegia, Chrysanthemum, Cineraria, Clover, Cosmo, Cowpea, Dahlia, Datura, Delphinium, Gerbera, Gladiolus, Gloxinia, Hippeastrum, Mesembryanthemum, Salpiglossis, Zinnia, and the like. In a prefeπed embodiment, the DNA is expressed in "seed crops" such as com, sweet com and peas etc. in such a way that the apomictic seed which results from such expression is not physically mutated or otherwise damaged in comparison with seed from untransformed like crops. Preferred are monocotyledonous plants of the Grammaceae family involving Lolium, Zea. Triticum. Tnticale, Somhum, Saccharum. Bmmus. On/zae. Avena. Hordeum. Secale and Setana plants. More preferred are transgenic maize, wheat, barley, sorghum, rye, oats, turf and forage grasses, millet and rice. Especially preferred are maize, wheat, sorghum, rye, oats, turf grasses and rice. Among the dicotyledonous plants Arabidopsis, soybean, cotton, sugar beet, sugar cane, oilseed rape, tobacco and sunflower are more preferred herein. Especially preferred are soybean, cotton, tobacco, sugar beet and oilseed rape. The expression 'progeny' is understood to embrace both, "asexually" and "sexually" generated progeny of transgenic plants. This definition is also meant to include all mutants and variants obtainable by means of known processes, such as for example cell fusion or mutant selection and which still exhibit the characteπstic properties of the initial transformed plant, together with all crossing and fusion products of the transformed plant material. This also includes progeny plants that result from a backcrossing, as long as the said progeny plants still contain the DNA according to the invention Another object of the invention concerns the proliferation material of transgenic plants. The proliferation material of transgenic plants is defined relative to the invention as any plant material that may be propagated sexually or asexually in vivo or in vitm. Particularly preferred within the scope of the present invention are protoplasts, cells, calli, tissues, organs, seeds, embryos, pollen, egg cells, zygotes, together with any other propagating material obtained from transgenic plants. Parts of plants, such as for example flowers, stems, fruits, leaves, roots oπginatmg in transgenic plants or their progeny previously transformed by means of the process of the invention and therefore consisting at least in part of transgenic cells, are also an object of the present invention. Espeically preferred a apomictic seeds. A further object of the invention is a method of producing apomictic seeds, but preferably seeds that are of the adventitious embryony type, comprising the steps of: (i) transforming plant material with a nucleotide sequence encoding a protein the presence of which in an active form in a cell, or membrane thereof, renders said cell embryogenic, but preferably a protein which is a protein kinase capable of spanning a plant cell membrane and capable of autophosphorylation. (ii) regenerating the thus transformed material into plants, or caφel-containing parts thereof, and (iii) expressing the sequence in the vicinity of the embryo sac. The kinase protein being expressed by the DNA according to the invention is preferably a leucine rich repeat receptor like kinase and comprises a ligand binding domain, a proline box, a transmembrane domain, a kinase domain and a protein binding domain. In a specific embodiment of the invention, the said kinase protein may tack a functional ligand binding domain but comprises a proline box, a transmembrane domain, a kinase domain and a protein binding domain. The genetic properties engineered into the transgenic seeds and plants described above are passed on by sexual reproduction or vegetative growth and can thus be maintained and propagated in progeny plants. Generally said maintenance and propagation make use of known agricultural methods developed to fit specific puφoses such as tilling, sowing or harvesting. Specialized processes such as hydroponics or greenhouse technologies can also be applied. As the growing crop is vulnerable to attack and damages caused by insects or infections as well as to competition by weed plants, measures are undertaken to control weeds, plant diseases, insects, nematodes, and other adverse conditions to improve yield. These include mechanical measures such a tillage of the soil or removal of weeds and infected plants, as well as the application of agrochemicals such as herbicides, fungicides, gametocides, nematicides, growth regulants, ripening agents and insecticides. Use of the advantageous genetic properties of the transgenic plants and seeds according to the invention can further be made in plant breeding which aims at the development of plants with improved properties such as tolerance of pests, herbicides, or stress, improved nutritional value, increased yield, or improved structure causing less loss from lodging or shattering. The various breeding steps are characterized by well-defined human intervention such as selecting the lines to be crossed, directing pollination of the parental lines, or selecting appropriate progeny plants. Depending on the desired properties different breeding measures are taken. The relevant techniques are well known in the art and include but are not limited to hybridization, inbreeding, backcross breeding, multiline breeding, variety blend, interspecific hybridization, aneuploid techniques, etc. Hybridization techniques also include the sterilization of plants to yield male or female sterile plants by mechanical, chemical or biochemical means. Cross pollination of a male sterile plant with pollen of a different line assures that the genome of the male sterile but female fertile plant will uniformly obtain properties of both parental lines. Thus, the transgenic seeds and plants according to the invention can be used for the breeding of improved plant lines which for example increase the effectiveness of conventional methods such as herbicide or pestidice treatment or allow to dispense with said methods due to their modified genetic properties. Alternatively new crops with improved stress tolerance can be obtained which, due to their optimized genetic "equipment" , yield harvested product of better quality than products which were not able to tolerate comparable adverse developmental conditions. In seeds production germination quality and uniformity of seeds are essential product characteristics, whereas germination quality and uniformity of seeds harvested and sold by the farmer is not important. As it is difficult to keep a crop free from other crop and weed seeds, to control seedborne diseases, and to produce seed with good germination, fairly extensive and well-defined seed production practices have been developed by seed producers, who are experienced in the art of growing, conditioning and marketing of pure seed. Thus, it is common practice for the farmer to buy certified seed meeting specific quality standards instead of using seed harvested from his own crop. Propagation material to be used as seeds is customarily treated with a protectant coating compπsing herbicides, insecticides, fungicides, bacteπcides, nematicides, molluscicides or mixtures thereof. Customarily used protectant coatings compπse compounds such as captan, carboxin, thiram (TMTD * ), methalaxyl (Apron*), and piπmiphos-methyl (Actellic*). If desired these compounds are formulated together with further carriers, surfactants or application- promoting adjuvants customarily employed in the art of formulation to provide protection against damage caused by bacterial, fungal or animal pests. The protectant coatings may be applied by impregnating propagation material with a liquid formulation or by coating with a combined wet or dry formulation. Other methods of application are also possible such as treatment directed at the buds or the fruit. It is thus a further object of the present invention to provide plant propagation material for cultivated plants, but especially plant seed that is treated with an seed protectant coating customarily used in seed treatment. It is a further aspect of the present invention to provide new agricultural methods such as the methods examplified above which are characterized by the use of transgenic plants, transgenic plant material, or transgenic seed according to the present invention. To breed progeny from plants transformed according to the method of the present invention, a method such as that which follows may be used: plants produced as described in the examples set forth below are grown in pots in a greenhouse or in soil, as is known in the art, and permitted to flower. Pollen is obtained from the mature stamens and used to pollinate the pistils of the same plant, sibling plants, or any desirable plant. Similarly, the pistils developing on the transformed plant may be pollinated by pollen obtained from the same plant, sibling plants, or any desirable plant. Transformed progeny obtained by this method may be distinguished from non-transformed progeny by the presence of the introduced gene(s) and/or accompanying DNA (genotype), or the phenotype conferred. The transformed progeny may similarly be selfed or crossed to other plants, as is normally done with any plant carrying a desirable trait. Similarly, tobacco or other transformed plants produced by this method may be selfed or crossed as is known in the art in order to produce progeny with desired characteristics. Similarly, other transgenic organisms produced by a combination of the methods known in the art and this invention may be bred as is known in the art in order to produce progeny with desired characteristics. Further comprised by the invention is a method of obtaining embryogenic cells in plant material, comprising transforming the material with a recombinant DNA sequence or a vector according to the invention, expressing the sequence in the material or derivatives thereof and subjecting the said material or derivatives to a compound which acts as a ligand for the gene product of the said sequence. The invention further relates to a method of generating somatic embryos under in vitm conditions wherein the SERK protein is overexpressed ectopically. The invention still further includes the use of the said DNA in the manufacture of apomictic seeds, in which use the sequence is expressed in the vicinity of the embryo sac. in a specific embodiment of the invention the SERK gene may be expressed in transgenic plants such as, for example, an Arabidopsis plant, under the control of plant expression signals, particularly a promoter which regulates expression of SERK genes in planta, but preferably a developmentally regulated or inducible promoter such as, for example, the carrot chitinase DcEP3-1 gene promoter, the Arabidopsis AtChitlV gene promoter, the Arabidopsis LTP-1 gene promoter, the Arabidopsis bel-1 gene promoter, the petunia fbp-7 gene promoter, the Arabidopsis ANT gene promoter, or the promoter of the 0126 gene from Phalaenopsis; the Arabidopsis AtDMCI promoter, or the pTA7001 inducible promoter. The promoters of the DcEP3-1 and the AtChit IV genes may be cloned and characterized by standard procedures. The DcSERK coding sequence (SEQ ID No. 2) is cloned behind the DcEP3-1 , the AtChit IV or the AtLTP-1 promoters and transformed into Arabidopsis. The ligation is performed in such a way that the promoter is operably linked to the sequence to be transcπbed. This construct, which also contains known marker genes providing for selection of transformed mateπal, is inserted into the T-DNA region of a binary vector such as pBIN19 and transformed into Arabidopsis. transformation into Arabidopsis is performed by the vacuum infiltration or root transformation procedures known to the skilled man. Transformed seeds are selected and harvested and (where possible) transformed lines are established by normal selfing. Parallel transformations with 35S promoter-SERK constructs and the entire SERK gene itself are used as controls to evaluate over-expression in many cells or only in the few cells that naturally express the SERK gene. The 35S promoter-SERK construct may give embryo formation wherever the signal that activates the SERK-mediated transduction chain is present in the plant. A testing system based on emasculation and the generation of donor plant lines for pollen carrying LTP1 promoter-GUS and SERK promoter-bamase is established. The same constructs (35S, EP3-1 , AtChitlV, AtLTP-1 and SERK promoters fused to the SERK coding sequence) are employed for transformation into several Arabidopsis backgrounds. These backgrounds are wild type, male sterile, fis (allelic to emb 173) and pπmordia timing (pt)-1 lines, or a combination of two or several of these backgrounds. The wt lines are used as a control to evaluate possible effects on normal zygotic embryogenesis, and to score for seed set without fertilization after emasculation. The ms lines are used to score directiy for seed set without fertilization. The fis lines exhibit a certain degree of seed and embryo development without fertilization, so may be expected to have a natural tendency for apomictic embryogenesis, which may be enhanced by the presence of the SERK constructs. The pt-1 line has superior regenerative capabilities and has been used to initiate the first stably embryogenic Arabidopsis cell suspension cultures. Combinations of several of the above backgrounds are obtained by crossing with each other and with lines containing ectopic SERK expressing constructs. Except for the ms lines, propagation can proceed by normal self ing, and analysis of apomictic traits following emasculation. A similar strategy is followed in which the ATChilV, AtLTP-1 and SERK promoters are replaced by the bel-1 and fbp-7 promoters as well by other promoters specific for components of the female gametophyte. Additional constructs are generated that have constitutive receptor kinase activity. Most of the receptor kinases of the SERK type act as homodimeric receptors, requiring autophosphorylation before being able to activate downstream signal transduction cascades. In many receptor kinases the extracellular domain serves as an inhibitor of the kinase domain in the ligand-free stage. This arrest is removed after binding of the ligand (Cadena and Gill, 1992). By introduction of a SERK construct, from which the extracellular ligand-binding domain has been removed, mutant homodimeric (in cells that do not have a natural population of SERK proteins) or heterodimeric (in cells that also express the unmodified forms) proteins can be generated with a constitutively activated kinase domain. This approach, when coupled to one of the promoters active in the nucellar region, results in activation of the embryogenic pathway in the absence of the activating signal. This may be an important alternative in cases where it is necessary or desirable to have activation of the SERK pathway only dependant on specific promoter activity and independent of temporal regulation of an activating signal. Introduction of SERK constructs that result in fertilization-independent-embryogenesis (fie) are tested in other species for their effect. In order to recognize the fie phenotype, the skilled man will use appropriate male sterile backgrounds. However, pollination is often necessary for apomixis of the adventitious embryony type, in order to ensure the production of endosperm. Whilst the present invention has been particularly described by way of the production of apomictic seed by heterologous expression of the SERK gene in the nucellar region of the caφel, the skilled man will recognize that other genes, the products of which have a similar structure/function to the SERK gene product, may likewise be expressed with similar results. Moreover, although the example illustrates apomictic seed production in Arabidopsis, the invention is, of course, not limited to the expression of apomictic seed-inducing genes solely in this plant. Moreover, the present disclosure also includes the possibility of expressing the SERK (or related) gene sequences in the transformed plant material in a constitutive - tissue non¬ specific manner (for example under transcriptional control of a CaMV35S or NOS promoter). In this case, tissue specificity is assured by the localized presence within the vicinity of the embryo sac of the ligand of the product of the said gene. Furthermore, the SERK (or related) gene products may interact with proteins such as transcπption factors which are involved in regulating embryogenesis. This interaction withtn tissue which has been transformed according to the present disclosure is also part of the present invenbon. The skilled man who has the benefit of the present disclosure will also recognize that the SERK gene (and others as indicated in the preceding paragraph) may be transformed into plant mateπal which may be propagated and/or differentiated and used as an explant from which somatic embryos can be obtained. Expression of such sequences in the transformed tissue (which is subjected to a ligand of the kinase gene products) substantially increases the percentage of the cells in the tissue which are competent to form somatic embryos, in compaπson with the number present in non-transformed like tissue. The invention will be further apparent from the following descπption and the associated drawings and sequence listings. SEQ ID NO. 1 depicts the Daucus carota genomic clone of the putative receptor kinase (SERK) associated with the transition of competent to embryogenic cells; SEQ ID NO. 2 depicts the cDNA of the said putative kinase; SEQ ID NOs. 3 depicts the the predicted protein sequence of the SERK protein encoded by the DNA of SEQ ID NO:1. SEQ ID NOs: 4-16 depict the sequences of vaπous PCR pπmers; and SEQ ID NOs. 17-19 depict specific peptides contained within the gene product of SEQ ID NO. 2. SEQ ID NO: 20 depitcts the Arabidopsis thaliana partial genomic clone of the putative receptor kinase (SERK) associated with the transition of competent to embryogenic cells. SEQ ID NO: 21 depicts the predicted protein sequence of the SERK protein encoded by the DNA of SEQ ID NO:20. SEQ ID NOs: 22, 24, 26, 28 and 30 depict the partial DNA sequences of 5 EST clones with high homology to the SERK LRR sequences . SEQ ID NOs. 23, 25, 27, 29 and 31 depict the predicted protein sequence of the partial DNA sequences of the 5 EST clones of SEQ ID Nos: 22, 24, 26, 28 and 30. SEQ ID NO: 32 depicts the nuclotide sequence of the SERK cDNA from Arabidopsis thaliana. SEQ ID NO: 33 depicts the predicted amino acid sequence of the SERK protein from Arabidopsis thaliana encoded by the DNA of SEQ ID NO: 32. Figure 1 shows the results of an RT-PCR experiment performed on RNA extracted from the indicated tissues. 40 cycles followed by Southern blotting of the resulting bands is necessary to visualize SERK expression. Lanes include explants at day 7, treated for less (lane 1 ) or more (lane 2) then 3 days with 2,4-D. In the original a very faint signal is visible in lane 2, but not in lane 1. Established embryogenic cultures (lanes 4-6) but not a non-embryogenic control (lane 3) express the SERK gene. In carrot plants, no expression is detectable except for developing seeds after pollination (lane 7). Up to day 7 after pollination, the carrot zygote remains undivided, suggesting that the observed signal is coming only from the zygote. At day 10, the early globular and at day 20 the heart stage is reached in carrot zygotic embryogenesis. No signals are seen on Northern blots. Figure 2A shows the results of a whole-mount in situ hybridization with the SERK cDNA on 7 day explants treated for 3 days with 2,4 D. Few cells on the surface of the explant express the SERK gene, and those cells that do are the ones that become embryogenic. Figure 2B shows a whole mount in situ hybridization on a partially dissected seed containing a globular zygotic embryo. Hybridization is visualized by DIG staining. Figure 3 shows SERK expression in embryogenic hypocotyl cells during hormone-induced activation, determined by whole mount in situ hybridization . Ban 50 mm (A-E) Cell population generated by mechanical fragmentation of the activated hypocotyls. Only few of a certain type of cell, defined enlarged cell show SERK expression (asterisks). Small cytoplasmic cells (c), enlarging cells (eg) and large cells (I) never show SERK expression. (F) Hypocotyl longitudinal section before hormone-induced activation. It is not possible to detect any SERK expression in any type of cell. (G-l) Proliferating mass coming from the inner hypocotyl tissues 10 days after the beginning of the hormonal treatment (longitudinal section). In G a single enlarged cells showing SERK expression is detectable within a row of negative ceils showing the same moφhology. In H a single enlarged cell showing serk expression is detaching from the surface of the proliferating mass. In I a cluster of enlarged cells showing SERK expression is detectable at the surface of proliferating tissue. (J) Proliferating mass coming from the inner tissues of the hypocotyl 10 days after the beginning of the rooting treatment (24 hours with 2,4-D followed by hormone removal). Both the root primordia and the enlarged cells detaching from the surface do not show any SERK expression. Figure 4 shows the phenotype of Arabidopsis WS plants transformed with the 2200 bp SERK- lucrferase consturct at the seedling level. Pictures were taken at 28 days after germination of T2 seeds. In plant II and III no clear shoot meπstem is visible at the seedling stage, 7 days after ger¬ mination. The first two leaves, if they develop at all, are needleshaped as hown on the pictures taken 28 days after germination. At this time plant I, which shows no clear phenotype, already starts floweπng. Secondary shoot meπstems are already developing in plant no II and will also develop later from no III. Shoot meπstems, influorescences and normal flowers eventually develop on all plants. Figure 5 shows how the 2200 bp SERK luciferase construct affects the number of developing ovules in the siliques of transformed plants. Figure 6 shows autophosphorylation of purified SERK fusion protein in vrtm. Lane 1: purified SERK fusion protein; Lane 2: seπne phosphate; Lane 3: threonine phosphate; Lane 4: thyrosine phosphate. The following descπption illustrates the isolation and cloning of the SERK gene and the production of apomictic seed by heterologous expression of the said gene in the nucellar region of the caφel so that somatic embryos form which penetrate the embryo sac and are encapsulated by the seed as it develops. ISOLATION AND CLONING OF THE SERK GENE FROM DAUCUS CAROTA isolation of cDNA clones that are preferentially expressed in embryogenic cell cultures of carrot In order to increase the chance of success for obtaining genes expressed in carrot suspension cells competent to form embryos, the number of embryo-forming cells as present in a series of established cell cultures was determined. A sub-population of cells that passed through a 30 mm nylon sieve was isolated from eight different cultures that ranged in age between 2 months and 4 years. In these sub 30 mm populations, the number of embryos formed from the single cells and small cell clusters was determined and expressed as a percentage of the total number of cells present at the start of embryogenesis. Sieved <30 mm cultures able to form somatic embryos with a frequency of more than 1% were then used as a source for competent cells, and cultures that produced less than 0.01% embryos were used as non-embryogenic controls. As main cloning strategies, cold plaque screening (Hodge et al. 1992) and differential display (dd) RT-PCR (Liang and Pardee, 1992) were used besides conventional differential screening of cDNA libraries. Labeled probes for differential screening were obtained from RNA out of a <30 mm sieved sub-population of cells from either embryogenic or non-embryogenic cell cultures. Employing these probes in a library screen of approximately 2000 plaques yielded 26 plaques that failed to show any hybridization to either probe. These so-called cold plaques were purified and used for further analysis. From the total number of plaques that did hybridize, about 30 did so only with the probe from embryogenic cells. ddRT-PCR reactions using a combination of one anchor primer and one decamer primer were performed on mRNA isolated from three embryogenic, and three non-embryogenic suspension cultures. About 50 different ddRT-PCR fragments were obtained from each reaction. Using combinations of three different anchor and six different decamer primers, a total of approximately 1000 different cDNA fragments was visualized. Six of these PCR fragments were only found in lanes made with mRNA from <30 mm populations of cells from embryogenic cultures (Table 1 ) and with oligo combinations of the anchor primer (5'- I I l l l l I I I I I GC-3') and the decamer primers (5 * -GGGATCTAAG-3'), (5-ACACGTGGTC-3'), (5'-TCAGCACAGG-3 r ). Because differential PCR fragments often consist of several unresolved cDNA fragments (Li ef al. 1994), cloning proved to be essential prior to undertaking further characterization of the PCR fragments obtained. All clones obtained were subjected to a second screen, that consisted of spot-dot Northern hybridization performed under conditions of high stringency. This method, that used RNA from entire unsieved embryogenic and non-embryogenic suspension cultures, proved to be a fast and reliable additional selection method. Only one clone (22-28) of the 30 clones obtained after differential screening, proved to be restricted to embryogenic cell cultures while the majority was constitutively expressed. The 26 clones obtained from the cold plaque screening required long exposure times in the spot-dot Northern analysis. Six of these clones failed to show any hybridization signal and 19 proved to be expressed in both embryogenic and non-embryogenic cell cultures. One clone (31-50) showed low expression in all embryogenic cultures, and in one non-embryogenic culture, but not in the others. Of the six cloned fragments obtained by ddRT- PCR display, four showed hybridization more or less restricted to transcripts present in embryogenic cultures. All clones that passed through the second screening were sequenced. Two of the ddRT-PCR clones (6-8 and 7-13) were identical to the carrot Lipid Transfer Protein (LTP) gene, previously identified as a marker for embryogenic carrot cell cultures. LTP expression is restricted to embryogenic cell clusters and the protoderm of somatic and zygotic embryos from the early globular stage onwards (Sterk et al. 1991). Therefore, while the LTP gene is not a marker for competent cells, its appearance in the screening confirms the validity of our methods with respect to the cloning of genes expressed eariy during somatic embryogenesis. cDNA clone 31-50 encodes a leucine-rich repeat containing receptor-like kinase The mRNA corresponding to the isolated clone 31-50 had an open reading frame of 1659 nucleotides encoding a protein with a calculated Mw of 55 kDa. Because clone 31-50 is mainly expressed in embryogenic cell cultures it was renamed Somatic Embryogenesis Receptor Kinase (SERK). The SERK protein contains a N-terminal domain with a five-times repeated leucine-rich motif that is proposed to act as a protein-binding region in LRR receptor kinases (Kobe and Deisenhofer, 1994). Between the extracellular LRR domain of SERK and the membrane-spanning region is a 33 amino acid region rich in proiines (13), that is unique for the SERK protein. Of particular interest is the sequence SPPPP, that is conserved in extensins, a class of universal plant cell wall proteins (Varner and Lin, 1989). The proposed intracellular domain of the protein contains the 11 subdomains characteristic of the catalytic core of protein kinases. The core sequences HRDVKAAN and GTLGYIAPE in respectively the kinase subdomains VB and VIII suggest a function as a serine / threonine kinase (Hanks et al. 1988). Another interesting feature of the intracellular part of the SERK protein is that the C-terminal 24 amino-acids resembles a single LRR. The serine and threonine residues present within the intracellular LRR sequence are surrounded by acidic residues and might be targets for the autophosphorylation of SERK, thereby regulating the ability of other proteins to interact with this receptor-kinase in a similar fashion as described for the SH2 domain of the EGF family of tyrosine receptor kinases. Hybridization of the SERK cDNA clone to the carrot genome revealed the presence of only a single main hybridizing band after digestion with EcoRI , probably reflecting a single SERK gene in the carrot genome. This was confirmed after digestion with Ddel, an enzyme that cuts three times within the SERK gene. No signal was observed after Northern blotting of mRNA from embryogenic cell cultures and hybridization with labeled SERK probes, reflecting the low levels of transcript present in these cultures. Detection of the SERK transcript on the original spot-dot Northerns was only possible after long exposure times compared with other probes. The ability of the SERK protein to autophosphorylate was investigated in vitm, using a previously described autophosphorylation assay (Mu et al. 1994), with a bacterial fusion protein that contained the complete intracellular region of the SERK protein. The bacterially expressed SERK fusion protein was able to autophosphorylate, indicating that the SERK protein is able to fulfill a role as a protein kinase in vivo (Heldin, 1995). Expression of the SERK gene corresponds with the first appearance of competent cells during hypocotyl activation When carrot hypocotyls are induced with 2,4-D, only the cells of the provascular tissue proliferate. Cells of epidermal and cortical origin merely expand, suggesting that the provascular tissue derived cells form the newly initiated suspension culture. After removal of 2,4-D, the formation of somatic embryos occurs after 2-3 weeks. Somatic embryos are preceded by embryogenic cells, that are developed in turn from competent cells. While competent and embryogenic cell formation take place in the presence of 2,4-D, it was not clear when this occurred, and which cells acquired competence. Since previous experiments (Toonen et al. 1994) revealed that cell moφhology is not a good criterion, the first appearance of single competent cells was determined experimentally by semi-automatic cell tracking performed on large populations of immobilized cells. Hypocotyl explants activated with 2,4-D for seven days were mechanically fragmented and samples of the resulting population of mainly single suspension cells were immobilized to allow recording of their development by cell tracking, tn the immobilized cell populations obtained in this way all the moφhologicaliy discernible cell types were present that were also seen in the un-fragmented activated hypocotyls. Because the different cell moφhologies observed duπng hypocotyl activation were known (Guzzo ef a/ 1995), it was possible to trace back the oπginal position of each type of cell in the activated explant. Small cytoplasm-πch cells (16x16 mm) are the proliferating cells that surround the vascular elements. Enlarging vacuolated cells (16x40 mm) are encountered on the surface of the mass of proliferating cells and these can detach from the surface when fully enlarged (35x90 mm). Large vacuolated cells (more than 60x140 mm) are the non-proliferating remnants of the hypocotyl epidermis and cortical parenchyma. The shape of the enlarging and fully enlarged cells could change from oval to elongate or tπangular. Cell tracking on a total of 24,722 cells released from seven days activated hypocotyls showed that only 20 single cells formed a somatic embryo. Because of their dependance on continued 2,4-D treatment, the embryo- forming single ceils are still in the competent cell stage. All of the embryo-forming single cells belonged to the category of 3,511 enlarged cells, that contained therefore competent cells in a frequency of 0.56%. The single cell tracking expeπments cleariy reveal that the ability of explant cells to reinitiate cell division under the influence of 2,4-D, resulting in a population of highly cytoplasmic and rapidly proliferating cells, does have a causal relation with the ability to become embryogenic. It is also clear that only a very limited number of the cells that make up the newly initiated embryogenic suspension culture are actually competent to form embryogenic cells. Expression of the SERK gene, determined by whole mount in situ hybπdization on a similar population of cells as used for the cell tracking expeπments, was found to be restπcted to only 0.44% of the enlarged cells. Therefore, the expression of the SERK gene appears closely correlated both qualitatively and quantitatively with the presence of competent single cells. To obtain insight into the temporal regulation of SERK expression in the course of explant activation, whole mount in situ hybridization was performed on entire intact or hand-sectioned explants treated for different periods with 2,4-D. Representative samples were collected at daily intervals from explants untreated and treated for three days, six days, seven days or ten days with 2,4-D before returning to B5-0. No SERK-expressmg cells were ever found in explants treated for less then three days with 2,4-D. While enlarged cells became present after the first five days of culture, the first few SERK-expressing enlarged cells were found after six-seven days of culture in the presence of 2,4-D treatment. These few cells were present at the surface - 22 - of the mass of proliferating cells originating from the provascular tissue. In the hypocotyls treated for ten days with 2,4-D, the number of SERK-positive cells had increased to 3.04% and included at this stage also ceils present in small clusters. No SERK transcript was ever detected in small cytoplasm-rich cells or large vacuolated cells. Hypocotyls were also treated for only one day with 2,4-D and subsequently cultured in hormone-free medium for a total of seven or ten days. Under these conditions explant celts proliferated and gave rise to roots and non-embryogenic cell cultures, while SERK expression could never be detected. The in situ hybridization results described above were obtained from a relatively small number of explants and a few hundred cells, so RT-PCR followed by Southern hybridization was performed to obtain more quantitative results. These are shown in Figure 7 and confirm the close temporal correlation between the first appearance of competent cells in explants treated for three days with 2,4-D and the expression of the SERK gene. Northern hybridization never gave any signal after hybridization with SERK cDNA probes, not even after prolonged exposure in a Phosphorimager, in line with the extremely restricted expression pattern of the SERK gene. Expression of the SERK gene corresponds with the occurrence of competent cells in established embryogenic cell cultures While the results described so far indicate that competent and embryogenic cell formation is restricted to a particular class of enlarged cells during explant activation, the situation in an established embryogenic cell culture is more complex. Competent single cells in such cultures do not appear to belong to one cell type in particular, but have been shown to originate from all moφhologically different cell types. In cell tracking experiments, embryogenic cells, that do not require exogenous auxin treatment, were never observed to be single but consisted of clusters of at least 3-4 cells (Toonen et al. 1994). SERK expression was found in all moφhologically discernible single cell types that were present in an embryogenic cell culture at a frequency between 0.1 and 0.5% depending on the cell type. In non-embryogenic cultures, SERK expressing cells were never encountered. As was observed in the activated explants, SERK expression was not restricted to single cells, but also occurred in small clusters of 2 to 16 cells. Since clusters of this size are known to consist of embryogenic cells, these data show that SERK expression is not restricted to competent single cells, but may persist in small clusters of embryogenic cells. No SERK expression was encountered during the late globular, heart and toφedo-stages of somatic embryogenesis. The SERK gene is transiently expressed in zygotic embryogenesis The expression of the SERK gene in carrot plants was determined by RT-PCR. The results indicate that no SERK mRNA accumulates in any of the adult plant organs nor in flowers prior to pollination. The first occasion when SERK expression can be detected is in flowers at three days after pollination (DAP), at which stage fertilization has taken place and endosperm development has commenced. SERK mRNA remains present in flowers up to twenty DAP, corresponding with the eariy globular stage of the zygotic embryo (Yeung et al. 1996). Whole mount in situ hybridization on partially dissected carrot seeds confirmed that the SERK gene was only expressed in eariy embryos up to the globular stage. Expression was observed in the entire embryo including the suspensor. No expression was seen in seedlings, roots, stems, leaves, developing and mature flower organs, pollen grains and stigma's before and after fertilization. Tissues in the developing seed such as seed coat, integuments, all embryo sac constituents before fertilization as well as the endosperm at all stages of development investigated did not show any SERK expression. Later stages of carrot zygotic embryos were also completely devoid of SERK mRNA. Given this pattern of expression, that is restricted to the zygotic embryo, the signal as detected by RT-PCR in flowers at 3 and 7 DAP must come from SERK mRNA as present in zygotes, because in carrot the zygote remains undivided up to one week after pollination (Yeung et al. 1996). Although SERK expression persists to slightly later stages in zygotic globular embryos when compared to the somatic ones, these results confirm the transient pattern of expression as observed for the SERK gene during somatic embryogenesis and also imply that there is a correspondence between the formation of competent cells in vitro and the fomiation of the zygote in vivo. METHODS Cell culture, hypocotyl explant induction and cell tracking Cell cultures were derived from Daucus camta cv. Flakkese and maintained as previously described (De Vries ef a/. 1988a). Cell suspension cultures were maintained at high cell density in B5 medium (Gamborg et al. 1968) supplemented with 2 mM 2,4-D (B5-2 medium). Embryo cultures with globular, heart and toφedo-stage somatic embryos were derived from <30 mm sieved cell cultures cultured at low cell density (100 000 cells / ml) in B5 medium without 2,4-D (B5-0). For hypocotyl explant induction experiments, plantlets were obtained from seed of Daucus camta cv. S Valery as described previously (Guzzo ef al., 1994). The hypocotyls of one week old plantlets were divided in segments of 3-5 mm, incubated for various periods of time in B5-2 medium and returned to B5-0 medium. Seven days after explantation and exposure to 2,4- D the hypocotyl segments were fragmented on a 170 mm sieve and the resulting cells collected to form a fine cell suspension. Immobilization of these cells in B5-0.2 medium was performed in a thin layer of phytagel (Toonen et al. 1994). After one week of further culture 2,4-D was removed by washing the plates with B5-0 medium. This allowed embryos to develop beyond the globular stage. Recording the development of the immobilized cells was performed with a procedure modified from the previously described by Toonen et al. (1994). The main change involved a new MicroScan program for automatic 3-axis movement to scan ali cells in the phytagel (Toonen et al. 1996). Nucleic acid isolation and analysis RNA was isolated from cultured cells and plant tissues as described by De Vries ef al. (1988b). Poly(A) + -RNA was obtained by purification by oligo (dT) cellulose (Biolabs). For RNA gel blot analysis samples of 10 mg total RNA were electrophoresed on formamide gel, and transferred to nytran-plus membranes. For RNA spot-blot analysis 5 mg of total RNA was denatured and spotted onto nytran-plus filters using a hybridot manifold (BRL). Genomic DNA was isolated according to Sterk et al. (1991). Samples of 10 mg genomic DNA were digested with different restriction enzymes and separated on agarose gel, and transferred to nytran-plus membrane (Schleicher & Schuell). Hybridization of RNA blots took place at 42°C in hybridization buffer containing 50% formamide, 6xSSC, 5xDenhardt, 0.5% SDS and 0.1 mg/ml salm sperm DNA. Hybridization of DNA blots was performed as previously described (Sterk et al. 1991). Following hybridization, filters were washed under stringent conditions (3x20 min in 0.1% SSC, 1% SDS, at 65°C). Filters were exposed to Kodak X-Omat AR film. The integrity and the amount of RNA on the blots was confirmed by hybridization with an 18S ribosomal RNA probe. Nucleotide sequence analysis was performed on an ABI 373A automated DNA sequencer (Applied Biosystem). Screening procedures Two independent cDNA libraries were constructed with equal amounts of poly(A) * -RNA from total established cell cultures grown for six days in B5-2 medium, sieved <125 mm cell cultures grown for six days in B5-0 medium and sieved <30 mm cell cultures grown for six days in B5-0 medium. cDNA synthesis and cloning into the Uni-ZAP™ XR vector was performed according to the manufacturers protocol (Stratagene). Differential screening of the cDNA libraries was performed essentially as described by Scott et al. (1991). RNA was isolated from either three embryogenic or three non-embryogenic cell cultures, that were grown for seven days in B5-2 after sieving through 30 mm mesh. First strand cDNA synthesis was performed on 4 mg total RNA using AMV reverse transcriptase (Gibco BRL). [ PJdATP labeled probes were prepared using random prime labeling on first strand cDNA. Pooled probes from embryogenic and non-embryogenic cell populations were hybridized to two pairs of nitrocellulose filters, each containing 1000 plaques from one cDNA library. After washing for 3x20 min in 0.1% SSC, 1% SDS at 65°C, hybridization was visualized by autoradiography for two days on Kodak X-omatic film. Plaques that only showed signal with the embryogenic transcript probe were purified by two further rounds of screening. In order to identify cDNA clones which are expressed at low levels in the <30 mm sieved cell population, cold plaque screening was performed as described by Hodge et al. (1992). Plaques from the differential screening that did not show any signal after seven days of autoradiography were purified by two further rounds of screening. The resulting clones were used as probes for characterization of the expression pattern of the corresponding genes. Differential Display RT-PCR Differential display of mRNA was performed essentially as described by Liang and Pardee (1992). cDNA synthesis took place by annealing 1 mg of total RNA in 10 ml buffer containing 200 mM KCl, 10 mM Tris-HCl (pH 8.3), and 1 mM EDTA with 100 ng of one of the following anchor primers: (5'- l 1 1 I I I I I I I I GC-3'), (5'- l I I I I I I I I I I CTG-3'), (5'- l I I I t i l l I I I CA-3'). Annealing took place by heating the mix for 3 min. at 83°C followed by incubation for 30 min at 42°C. Annealing was followed by the addition of 15 ml pre-warmed cDNA buffer containing 16 mM MgCI 2 , 24 mM Tris-HCl (pH 8.3), 8 mM DTT, 400 mM dNTP, and 4 Units AMV reverse transcriptase (Gibco BRL). cDNA synthesis took place at 42°C for 90 min. First strand cDNA was phenol/chlorophorm extracted and precipitated with ethanol using glycogen as a carrier. The PCR reaction was performed in a reaction volume of 20 ml containing 10% of the synthesized cDNA, 100 ng of anchor primer, 20 ng of one of the following 10-mer primers: (5- GGGATCTAAG-3') , (5'-TCAGCACAGG-3'), (5'-GACATCGTCC-3') ( (δ'-CCCTACTGGT-S'), (5'- ACACGTGGTC-3'), (5'-GGTGACTGTC-3'), 2 mM dNTP, 0.5 UnrtTag enzyme in PCR buffer (10 mM Tπs-HCI (pH 9.0), 1.5 mM MgCI 2 , 50 mM KCl, 0.01% gelatin and 0.1% Tπton X100) and 6 nM [a- 32 ?] dATP (Amersham). PCR parameters were 94°C for 30 sec, 40°C for 1 mm, and 72°C for 30 sec for 40 cycles using a Cetus 9600 (Perkin-Elmer). Amplified and labeled cDNAs were separated on a 6% denatuπng DNA sequencing gel. Gels were dπed without fixation and bands were visualized by 16 hours of autoradiography using Kodak X-omatic film. Bands containing differentially expressed cDNA fragments of 150-450 nucleotides were cut out of the gel and DNA was extracted from the gel slices by eiectroelution onto DE-81 paper (Whatmann). After washing of the paper in low salt buffer (100 mM LiCI 2 in 10 mM TE buffer), and elution of the cDNA in high salt buffer (1 M LICI 2 in 10 mM TE buffer with 20% ethanol) the cDNA was concentrated by precipitation in ethanol using glycogen as earner. Reampirfication of the cDNA fragments using the same PCR cycling parameters as descπbed above but PCR buffer containing 2.5 mM of both the 10-mer and the anchor oligo and 100 mM dNTP. DE-81 paper allowed an efficient recovery of the DNA fragments and reampirfication generated an average of 500 ng DNA after 40 cycles. Amplified PCR products were blunt-ended using the Klenow fragment of E.coli DNA Polymerase I (Pharmacia), purified on Sephacryl-S200 columns (Pharmacia), ligated into a Smal linearized pBluescπpt vector II SK " (Stratagene) and transformed into E coli using electroporation. RT-PCR Adult plant tissues from Daucus camta were obtained from S&G Seeds (Enkhuizen). Controlled pollination was performed by hand. Flower tissue RNA was obtained from three compete umbels for each time-point and contained all flower organs including pollen grains. 2 mg of total RNA from adult plant tissue or cell cultures was annealed at 42°C with 50 ng oligo (5'- TCTTGGACCAGATAATTC-3') in 10 ml annealing buffer (250 mM KCl, 10 mM Tris-HCl pH 8.3, 1 mM EDTA). After 30 mm. annealing, 1 unit AMV-reverse transcπptase was added in a volume of 15 ml cDNA buffer (24 mM Tris-HCl pH 8.3, 16 mM MgCI 2 , 8 mM DTT, 0.4 mM dNTP). The reverse transcπption reaction took place for 90 mm. at 42°C. PCR amplification of SERK-cDNA was earned out with two specific oiigos for the SERK kinase domain, (5'- CTCTGATGACTTTCCAGTC-3') and (5'-AATGGCATTTGCATGG-3'). Amplification was earned out with 30 cycles of 30 sec. at 94°C, annealing at 54°C for 30 sec. and extension at 72 β C for 1 mm., followed by a final extension for 10 mm.at 72°C. Whole mount in situ hybridization Whole mount in srtu hybπdizations were performed essentially as previously descπbed (Engler et al. 1994). Cell cultures and somatic embryos were immobilized on poly-L-lysme coated glasses duπng fixation to improve handling. Whole mount in situ hybπdization on explants took place by embedding hypocotyls from seven-days old plantlets in 3% Seaplaque agarose (Duchefa) and processing them in Eppendorf tubes. Transverse as well as longitudinal sections were made with a vibrotome (Biorad Microcut). Sections of 50-170 mm thick were incubated in B5-2 medium for a minimum of three days to induce formation of embryo-forming cells. Optimal induction was achieved with longitudinal hypocotyl sections with a thickness of at least 90 mm. To obtain proliferating, non-embryogenic cell cultures, hypocotyl sections were exposed to 2,4-D for onty 1 day, and subsequently transferred to B5-0 medium (Guzzo et al 1994). Whole mount in situ hybπdization on developing seeds was performed by removing the chalazal end of the seeds to allow easier probe penetration After hybπdization, the enveloping layers of integuments and endosperm were carefully removed to expose the developing embryos, tn situ hybπdization on sections was performed as descπbed previously (Sterk et al. 1991) except for the use of non- radioactive probes. All samples were fixed for 60 mm in PBS containing 70 mM EGTA, 4% paraformaldehyde, 0.25% glutaraldehyde, 0 1% Tween 20, and 10% DMSO. Samples were then washed, treated with proteinase K for 10 mm, again washed and fixed a second time. Hybπdization solution consisted of PBS containing 0.1% Tween 20, 330 mM NaCl, 50 mg/ml hepaπn, and 50% deionized formamide. Hybπdization took place for 16 hours at 42°C using digoxigenm-labeled sense or antisense πboprobes (Boehπnger Mannheim). After washing the cells were treated with RNaseA, and incubated with anti-digoxigenin-alkalme phosphatase conjugate (Boehπnger Mannheim) which had been preabsorbed with a plant protein extract. Excess antibody was removed by washing followed by πnsmg in staining buffer (100 mM Tπs-HCI pH 9.5, 100 mM NaCl, 5 mM MgCI 2 , 1 mM levamisole) and the staining reaction was performed for 16 hours in a buffer containing NBT and BCIP. Observations were performed using a Nikon Optiphot microscope equipped with Nomarski optics. Autophosphorylation assay A 1.4 kB Sspl cDNA fragment of the SERK cDNA encoding most of the open reading frame apart trom the N-terminal three LRRs was cloned into the pGEX expression vector (Pharmacia). A fusion protein consisting of SERK and the glutathione S-transferase gene product was synthesized by a three hours induction of transformed E.coli with 2 mM IPTG. Fusion protein was isolated and purified as described previously (Horn and Walker, 1994). Purified fusion protein was coupled to glutathione agarose beads (Sigma) and incubated for 20 min. at 20°C in a volume of 10 ml buffer 50 mM Hepes (pH 7.6), 10 mM MgCI 2 , 10 mM MnCI 2l 1 mM DTT, 1 mCi [y -^P] (3 000 Ci/mmol) . Excess label was removed by washing the fusion protein/glutatione agarose beads three times for 5 min. in 50 mM Tris-HCl (pH 7.3), 10 mM MgCI 2 at 4°C. Protein was removed from the beads by cooking in SDS-PAGE loading buffer. Equal amounts of protein were separated by SDS-PAGE and protein autophosphorylation was visualized by autoradiography. SERK fusion proteins produced with the Baculovirus expression system. Further fusion proteins containing the intracellular part of the Daucus camta SERK protein (1.0 kB Hindlll / Sspl fragment of the carrot SERK cDNA clone 31-50) were made using the baculorvirus vector pAcHLT. In vitm phosphorylation studies with this purified protein showed that most if not all of the autophosphorylation of this SERK fusion protein was at threonine residues (Figure 6) Construction of viral transfer vectors The pAcHLT-B and pAcHLT-C baculovirus transfer vectors were used for the cloning of two cDNA fragments of the carrot SERK gene. The Sspl 1.41 kB fragment of carrot DcSERK cDNA was cloned into the Smal site of pAcHLT-B and the Sspl / Pvull 1.07 kB fragment of carrot DcSERK cDNA was cloned into the Smal site of pAcHLT-C. The first construct contains the complete C-terminal part of the DcSERK protein and from the putative extracellular region the proline-rich region and three of the lecuine-rich repeats. The second construct contains only the putative intracellular region of the DcSERK gene product. Nucleotide sequence analysis was performed in order to confirm the presence and the orientation of the DcSERK cDNA within the vector. Transformation of insect cells The resulting transfer vectors were used to transfect (lipofect) insect cell culture Sf21 from Spodoptera frugiperda in combination with linearized AcMNPV baculovirus DNA. Monolayers of SF21 ceils were transfected in 35 mm petridishes containing 2 ml of Hink's medium. One microgram of linearized AcMNPV baculovirus DNA (Baculogold, Invitrogen) was added to 5 microgram of pAcHLT / SERK vector construct in 25 microliter of water. Fifteen microliter of Lipofectin (BRL) was mixed with 10 microliter of water, after which the DNA solution was added. After mixing 200 microliter of Hink's medium was added to the mix and the solution was transferred to the cell monolayer, from which the medium was removed. After one hour, 500 microliter of Hink's medium was added and the cells were incubated for anotehr 3 hours. Finally, 1 ml of Hink's medium with 20% foetal bovine serum (FBS) was added and the cells were incubated for 4 days. After transfection, the viral infection could be identified by the reduced growth of cells, the swollen shape and the enlarged nucleus. After four days, infected cells were harvested and the medium containing infectious budded virus was collected and used for plaque assays and amplification of recombinant virus stocks. Isolation of single recombinant viruses Single recombinant virus plaques were isolated from monolayers of cells infected with a titration range of the primairy virus stock. Infections was performed in 35 mm petridishes with monolayers of cells. Virus stocks were diluted in 600 microlieter of Graces medium and added to the cell monolayer, followed by a 90 minutes incubation period at in Graces medium with 20% FBS. Afterwards, 3% Sea Plaque agarose was autoclaved, mixed with an equal amount of 2x Graces medium with 20% FBS and from the resulting agarose overlay solution 2 ml. was spread over the cell monolayers after removal of the viral inoculum. After 4 days of incubation single plaques could be visulalized and purified for further analysis. Fusion protein production. After determining the titer of purified recombinant viruses, monolayers of Sf21 cells in 75 cm 2 flasks were infection with a multiplicity of infection (MOI) of 10. Incubation of cells with the virus inoculum was performed for 90 min. after which 8 ml. of Hink's medium with 10%FBS was added. After 3 days of incubation, cells were harvested and washed twice with PBS. Cells were lysed for 45 min on ice in twenty volumes of 1x insect cell lysis buffer (10 mM Tris pH 7.5, 130 mM NaCl, 1% Triton, 100 mM NaF, 10 mM NaPi, 10 mM NaPPi, with proteinase inhibitors: 16 mg/l benzamidine, 10 mg/l phenanthroline, 10 mg/l aprotinin, 10 mg/l leupeptin, 10 mg/l pepstatin A, 1 mM PMSF). The lysate was cleared by centrifugation at 10.000 g for 30 min and the supernatant was batchwise incubated in TALON resin (with high affinity for the 6xHIS tag of the recombinant fusion protein). Binding was performed by gentle agitation for 20 min. at room temp. The resin was washed three times with lysis buffer, followed by an elution step with lysis buffer with 200 mM imidazole. Purified fusion protein was collected and purifty and integrity was tested by SDS-PAGE. Autophosphorylation assays Protein kinase activity was detemined by incubating 1 microgram of purified fusion protein for 30 min. at room temp, in a buffer containing 10 mM MgCI2, 10 mM MnCI2, 1 mM DTT and 10 μM [gamma-32]ATP (105 pm/pmol ATP). The autophosphorylated fusion protein was purified after SDS-PAGE from the gel in a buffer containing 50 mM NH4C03, 0.1 % SDS, 0.25% beta-mercaptoethanol. Protein was precipitated with 20 μg/ml BSA and 20% (w/v) solid trichloroacetic acid. The precipitate was collected after centrifugation, hydrolysed in 50 μl 6N HCI for 1 hour at 120 degrees Celcius. HCI was subsequently removed by lyophilization and the pellet was resuspended in a buffer consiting of 2.2% formic acid and 7.8% acetic acid. Hydrolysed protein was loaded onto cellulose thin layer chromatography plates together with control amino acid samples (phosphoserine, phosphothreonine, phosphotyrosine). Chromatography was performed in a buffer containing propionic acid: 1M ammonium hydroxide: isopropyl alcohol (90:35:35 v/v/v). After separation and drying of the plates, the separated amino-acids were visualized by spraying with 0.25% ninhydrin in aceton, followed by heating for 5 min. at 65 degrees Celcius. Plates were afterwards exposed to Phospho Imager casettes in order to detect the phospho-labeled aminoacids. SERK antibodies Purified fusion proteins (10 μg) were mixed in complete Freund adjuvant and injected IP into BALBc mice. After 4 weeks booster antigen was injected (10 μg purified fusion protein in imcomplete Freund adjuvant). Two weeks later a final booster was injected. One week after the final booster, serum was collected from these mice. The specificity and the titer of the resulting sera was tested on Western blots using total insect cell extracts with or without the SERK fusion proteins. INTRODUCTION OF THE SERK GENE INTO PLANTA AND THE PRODUCTION OF APOMICTIC SEED Carrot transformation with a SERK promoter fraαment/luciferase oene fusion The binary vector pMT500 is based on the pBIN19 vector (Bevan, 1984) and contains the firefly luciferase gene downstream of a polylinker containing 5 unique restriction sites was created by uni-directional ligation of the firefly luciferase coding region followed by the polyadenylation sequence from the pea rbcS::E9 gene in the H/πdlll-Xoal site of the binary vector pMOGΘOO (kindly provided by Mogen N.V., Leiden, The Netherlands). The binary vector pMOGΘOO is based upon pBIN19 (Bevan, 1984) but while in pBIN19 the polylinker is flanked by the left border and the neomycin phosphotransferase (NPT II) expression cassette, the polylinker in pMOG800 is flanked by the right border and the NPT II expression cassette. From a genomic lambda clone, transcription regulating sequences from the carrot SERK gene were isolated by digestion with H/ndlll and Dral (SEQ ID No. 1), and cloned into the Hindlll / Smal sites of pBluescript SK+. From the resulting vector a Kpnl / Sstl fragment containing the SERK genomic DNA was isolated and cloned into the Kpnl / Sstl sites of the binary vector pMT500. The resulting DNA construct, pMT531 , contained the 2200 bp genomic SERK DNA fragment as promoter sequence, the luciferase gene as vital reporter, and the E9 transcription terminator sequence. The binary vector pMT531 was transformed by electroporation into Agmbacterium tumefaciences strains MOG101 and MOG301 (for transformation into carrot cells) and into Agmbacterium tumefaciences strain C58C1 (for transformation into Arabidipsis thaliana plants). Transformed colonies were selected on LB plates with 100mg/l kanamycin. Transformation of carrot cells The firefly luciferase coding sequence under control of the genomic carrot Hindlll / Dral 2200 bp DNA fragment was introduced into carrot cells by Agmbacterium tumefaciens mediated transformation of hypocotyl segments. Transformation of Daucus camta cv. 'Amsterdamse bak' was performed by slicing one week old dark grown seedlings into segments of 10 to 20 mm. Segments were incubated for 20 minutes in a freshly prepared 10 fold diluted overnight culture of Agmbacterium.. The segments were dried and transferred to a modified Gamborgs B5 medium (P1 medium; S&G seeds, Enkhuizen, The Netherlands) supplemented with 2 μM 2,4-D (P1-2) and solidified with agar (Difco, Detroit, Mi, USA ). After two days of culture in the dark at 25 ± 0.5 _C, segments were transferred to solidified P1-2 medium supplemented with kanamycin (100 mg -I "1 ), carbenicillin (500 mg-l" 1 ; Duchefa) and vancomycin (100 mg l "1 ; Duchefa). After three weeks segments were transferred to fresh plates and transformed calli were selected after an additional three weeks. Transformed calli were grown on P1-2 plates with antibiotics for 3 weeks at a 16 hour light/8 hour darkness regime. Transformed embryogenic suspension cultures were initiated as described by transferring 0.2 g callus to 10 ml liquid P1-2 medium supplemented with 200 mg -l" 1 kanamycin, 250 mg-l" 1 carbenicillin and 50 mg-l "1 vancomycin. During the first weeks 1 to 3 volumes of fresh medium were added to the culture at weekly intervals. After 5 to 7 weeks cultures were subcultured to a packed cell volume of 2 ml per 50 ml medium every two weeks and incubated at a 16 hour light / 8 hour darkness regime at 25 ± 0.5 °C. One week after transfer to kanamycin selection medium, hypocotyl segments were sprayed with lucifeπn to test whether luciferase expression could be detected in transformed callus shortly after transformation. A large number of hypocotyl segments showed luciferase activity at the cut edges, but did not develop calli. Instead, growth of bacteria occurred, suggesting that the luciferase activity was of bactenal origin. Six to ten weeks after transformation, calli were obtained that showed luciferase activity in variable amounts, while no bacterial growth could be observed anymore. After 12 weeks, calli measuring 5 to 10 mm in diameter were used to start suspension cultures. At this time no bactenal contamination was observed. A control transformation experiment in which luciferase expression under influence of the CaMV 35S promoter was observed in single cells and cell clusters in the suspension culture demonstrating that the luciferase protein is active in Daucus camta suspension cultured cells. Cell immobilisation One-week old high-density (10 6 - 10 7 cells-ml" 1 ) suspension cultures were sieved through nylon sieves with successive 300, 125, 50 and 30 μm pore sizes (Monodur-PES; Verseidag Techfab, Watbeck, Germany). Single cells and cell clusters passing the last sieve are designated as < 30 μm populations. Control experiments with untransformed cells were performed with Daucus camta cv. Trophy' (S&G seeds) suspension cultures grown in P1-2 medium. Size fractionated cell populations smaller then 30 μm were immobilised in phytagel (P8196; Sigma, St Louis, Mo, USA) in petnperm dishes (Heraeus, Hanau, Germany). The bottom layer consisted of 1 ml P1-0 medium with 5 mM Ca 2 + and 0.2 % phytagel. Two hundred thousand cells (< 30 μm and < 50 μm populations) in B5-0 medium without Ca 2+ supplemented with 0.1 % phytagel were poured on top of the bottom layer. For this layer B5 was applied since, at room temperature, phytagel solidified in P1 medium without Ca 2+ . After 2 hours of solidification an additional P1-0 layer with 0.2 % phytagel was poured onto the cell layer preventing the B5 layer to move. To prevent dehydration of the phytagel layers and to supply lucifenn to the cells, 0.5 ml P1-0 medium containing 0.05 μM luciferin (Promega, Madison, Wi, USA) was added after solidification. The final luciferin concentration in the culture was 0.02 μM. Luciferin detection on single cells was determined with a CCD camera for a period of 5 times one hour (Schmidt et al. (1997) Development 124: 2049-2062). After 7 days of culture, luciferin was removed from the cultures by extensive washing with P1 -0 medium. A rabidoosis transformation with a SERK promoter fraαment/luciferase gene fusion Wildtype WS plants were grown under standard long day conditions: 16 hours light and 8 hours dark. The first emerging mfluorescense was removed in order to increase the number of mfluorescenses. Five days later, plants were ready for vacuum infiltration. Agrobacterium strain C58C1 containing the transformation plasmid was grown on a LB plate with 50 mg/l kanamycin, 50 mg/l rifampicin and 25 mg/l gentamycin. A single colony was used to inoculate 500 ml of LB medium containing 50 mg/l kanamycin, 50 mg/l rifampicin and 25 mg/l gentamycin. The cultures were grown O/N at 28 degrees Celcius and the resulting log phase culture (OD6000.8) was centrifuged to pellet the cells and resuspended in 150 ml of infiltration medium (0.5x MS medium (pH 5.7) with 5% sucrose and 10 μl/l benzylaminopuπne). The inflorescenses of 6 Arabidopsis plants are submerged in the infiltration suspension while he remaining parts of the plants (which are still potted) are placed upside down on meshed wire to avoid contact with the infiltration suspension. Vacuum is applied to the whole set-up for 10 min. at 50 kPa. Plants are directly afterwards placed under standard long day conditions. After completed seed setting the seeds were surface sterilized by a 1% sodium hypochlorite soak, then thoroughly washed with sterile water and plated onto petridishes with O.δxMS medium and 80 mg/l kanamycin in order to select for transformed seeds. After 5 days germination under long day conditions (10.000 lux), the transformed seedlings could be identified by their green color of their cotyledons (the untransformed seedlings turn yellow), and were further grown in soil under C1 lab conditions under long day conditions. This vacuum infiltration method resulted in approximately 0.1% transformed seeds. Transformation of a construct containing both a gene encoding kanamycin resistance and the 2200 bp (Hindlll / Dral) SERK genomic DNA fused to the firefly luciferase gene into Arabidopsis thaliana (WS) by vacuum infiltration resulted in six different kanamycin-resistent primary transformants (I, II, III, IV, V and VI). Plants IV and VI died at the seedling stage, although they were kanamycin resistant. A T2 generation could be obtained from the four plants I, II, III and V (Figure 4). Within the siliques of the T2 generation of plants no. Ill and V, an early inhibition in development could be observed in appoximatetely 25-50 % of the seeds. The plants I and II did not show a reduction in the number of developing seeds.(Figure 5). Similar results were observed in a T3 generation, in which again approximately 25-50% of the seeds showed an early inhibition of normal seed development. Arabidopsis transformation with a AtSERK αene Isolation of the AtSERK genomic and cDNA clones Using the DcSERK cDNA sequence (seq ID no. 2) as a probe, a lambda ZipLox genomic library made form Arabidopsis Landsberg erecta total genomic DNA is screened for the presence of homologous sequences. Three different lambda clones with inserts of 14, 18 and 20 kb respectively are obtained. The 14 kb clone is digested by EcoRI and the resulting fragments subcloned into pBluescript vectors. Fragments spanning the entire coding sequence of the AtSERK gene are isolated, sequenced and compared with the Daucus homologues. The resulting sequence is shown as SEQ ID NO: 20. Using the DcSERK cDNA sequence (SEQ ID NO: 2) as a probe, a lambda ZAPII cDNA library is screened tor the presence of homologous sequences. Four lambda clones are obtained and their inserts subcloned into pBluescript vectors using the helper phage excision procedure. Fragments spanning the entire AtSERK cDNA coding sequence of the AtSERK gene are isolated, sequenced and compared with the Daucus homologues. The resulting sequence is shown as SEQ ID NO: 32. Plasmids containing promoter sequences Arabidopsis thaliana LTP1 promoter fragment is obtained from the binary plasmid pUHIOOO (Thoma, S., Hecht, U., Kipper, A., Borella, J., De Vries, S.C., Sommerville, C. (1994) Plant Physiol. 105, 35-45) by digestion with BamHI and H/ndlll and cloning into pBluescript SK " (pMT121). - The CaMV 35S promoter enhanced by duplication of the -343 to -90 region (Kay ef al., (1987) Science 236: 1299-1302) is isolated from the pMON999 vector by digestion with W/ndlll and Sstl and cloned into the pBluescript SK " vector (pMT120). - The promoter AtDMCI (Klimyuk and Jones (1997) Plant Journal 11 : 1-14). Plasmid SLJ 9691 is a construct consisting of pBluescript SK+ in which the Arabidopsis thaliana DMC1 genomic clone (accession number U76670) is cloned into the EcoRV site. SLJ 9691 carries EcoRV fragments of the 5' end of the AtDMCI gene with the following modification: a Bglll site instead of the second Hpal site, two ATG codons in the first exon and an Xhol site at the ATG codon of the second exon. - The FBP7 promoter from Petunia (Angenent et al. (1995) Plant Cell 7: 1569-1582). The promoter of the FBP7 gene is cloned by subcioning the 0.6 kb H/ndlll - Xbal genomic DNA fragment of FBP7 into the H/πdlll - Xbal site of pBluescript KS-, resulting in the vector FBP201. The pAtSERK binary vector constructs. Based on the pBIN 19 vector, a binary vector pAtSERK is constructed for transformation of the Arabidopsis thaliana SERK cDNA under the control of different promoters. The full length Arabidopsis thaliana cDNA clone of SERK (Seq ID No. NEW) is obtained from a pBluescript SK- plasmid. A Smal - Kpnl 2.1 kb fragment containing the AtSERK cDNA is cloned into pBIN19 Smal - Kpnl. The polyadenylation sequence from the pea rbcS::E9 gene (Millar et al., 1992), Plant Cell 4: 1075-1087) is placed downstream from the AtSERK cDNA by cloning a Klenow-filled EcoRI - Hindlll E9 DNA fragment into the Klenow- filled Xmal site of the pBIN19:AtSERK vector in order to generate the binary vector pAtSERK. Construction of plant expression vectors The pAtSERK binary vector is used to generate the following promoter-AtSERK constructs. - The AtLTPI promoter is cloned in the Smal site of the pAtSERK binary vector as a Klenow-filled Kpnl-Ssπ * DNA fragment to give the pAtLTPI AtSERK vector. - The CaMV 35S promoter is cloned in the Smal site of the pAtSERK binary vector as a Klenow-filled Kpπl-Ssfl fragment to give the p35SAtSERK vector. - The AtDMCI promoter consisting of the Bglll - Xhol 3.3kB fragment from the clone SLJ 9691 is filled in with Klenow and cloned into the Smal site of the pAtSERK binary vector to give the pAtDMCl AtSERK vector. - A Sacl-Kpnl fragment of FBP2101 is filled in with Klenow and cloned into the Smal site of the pAtSERK binary vector to give the pFBP2101 AtSERK vector. Introduction of plant expression vectors into Arabidopsis thaliana plant ceils The above described vector constructs (pAtLTPI AtSERK, p35SAtSERK, pAtDMCl AtSERK, pFBP2101 AtSERK) have been electrotransformed into Agmbacterium tumifacienses strain C58C1 as known in the art. Wild type Arabidopsis thaliana WS plants are grown under standard long day conditions: 16 hours light and 8 hours dark. The first emerging inflorescence is removed in order to increase the number of influorescences. Five days later, plants are ready for vacuum infiltration. Agrobacterium strain C58C1 containing the transformation plasmid (the pAtLTPI AtSERK vector or the p35SAtSERK or the pAtDMCl AtSERK vector or the pFBP2101 AtSERK vector) is grown on a LB plate with 50 mg/l kanamycin, 50 mg/l rifampicin and 25 mg/l gentamycin. A single colony is used to inoculate 500 ml of LB medium containing 50 mg/l kanamycin, 50 mg/l rifampicin and 25 mg/l gentamycin. The cultures are grown O/N at 28 degrees Celsius and the resulting log phase culture (OD6000.8) is centrifuged to pellet the cells and resuspended in 150 ml of infiltration medium (0.5x MS medium (pH 5.7) with 5% sucrose and 1 mg/l benzylaminopurine). The inflorescences of 6 Arabidopsis plants are submerged in the infiltration suspension while the remaining parts of the plants (which are still potted) are placed upside down on meshed wire to avoid contact with the infiltration suspension. Vacuum is applied to the whole set-up for 10 mm. at 50 kPa. Plants are directly afterwards placed under standard long day conditions. After completed seed setting the seeds are surface sterilized by a 1% sodium hypochloπte soak, then thoroughly ished with steπle water and plated onto petridishes with 0.5xMS medium and 80 mg/l kanamycin in order to select for transformed seeds. After 5 days germination under long day conditions (10.000 lux), the transformed seedlings could be identified by their green colour of their cotyledons (the untransformed seedlings turn yellow), and are further grown in soil under long day conditions. This vacuum infiltration method resulted in approximately 0.1% transformed seeds. Expression of SERK sequences in Arabidopsis thaliana plant cells The inflorescences from transgenic and not transgenic Arabidopsis thaliana plants are analysed by Whole mount in situ hybridisation analysis with AtSERK cDNA as probe. The inflorescences in different stages of development are fixed for 60 mm. in PBS containing 70 mM EGTA, 4% paraformaldehyde, 0.25% glutaraldehyde, 0.1% Tween 20, and 10% DMSO. Samples are then washed, treated with protemase K for 10 mm, again washed and fixed a second time. Hybπdisation solution consisted of PBS containing 0 1% Tween 20, 330 mM NaCl, 50 mg/ml hepaπn, and 50% deionized formamide. Hybπdisation took place for 16 hours at 42°C using digoxigenm-labeled sense or antisense πboprobes (Boehπnger Mannheim). After washing, the cells are treated with RNaseA and incubated with anti-digoxigenin-alkalme phosphatase conjugate (Boehπnger Mannheim) which had been preabsorbed with a plant protein extract. Excess antibody is removed by washing followed by πnsing in staining buffer (100 mM Tπs-HCI pH 9.5, 100 mM NaCl, 5 mM MgCI 2 , 1 mM levamisole) and the staining reaction is performed for 16 hours in a buffer containing NBT and BCIP. Observations are performed using a Nikon Optiphot microscope equipped with Nomarski optics. The transformed plants show ectopic expression of SERK in the vicinity of the embryo sac. SEQUENCE LISTIMG (1) GENERAL INFORMATION: (i) APPLICANT: (A) NAME: NOVARTIS AG (B) STREET: Schwarzwaldallee 215 (C) CITY: Basel (E) COUNTRY: Switzerland (F) POSTAL CODE (ZIP) : 4058 (G) TELEPHONE: +41 61 69 11 11 fl (H) TELEFAX: + 41 61 696 79 76 (I) TELEX: 962 991 (ii) TITLE OF INVENTION: Iπproveπients in or relating to organic cαrpounds (iii) NUMBER OF SEQUENCES: 33 (iv) COMPUTER READABLE FORM: (A) MEDIUM TYPE: Floppy disk (B) COMPUTER: IBM PC cαπpatible (C) OPERATING SYSTEM: PC-DOS/MS-DOS (D) SOFTWARE: Patentln Release #1.0, Version #1.25 (EPO) (2) INFORMATION FOR SEQ ID NO: 1: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 6695 base pairs (B) TYPE: nucleic acid (C) STRANDEI-NESS: double (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: ENA (genomic) (iii) HYPOTHETICAL: NO (iii) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (A) ORGANISM: Daucus carota (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 3696..6617 (ix) FEATURE: (A) NAME/KEY: intron (B) LOCATION: 3731..3802 (ix) FEATURE: (A) NAME/KEY: nitron (B) LOCATION: 3851..3979 (ix) FEATURE: (A) NAME/KEY: intron (B) LOCATION: 4124..4211 (ix) FEATURE: (A) NAME/KEY: intron (B) LOCATION: 4284..4357 (ix) FEATURE: (A) NAME/KEY: intron (B) LOCATION: 4430..4528 (ix) FEATURE: (A) NAME/KEY: intron (B) LOCATION: 4642.-4757 (ix) FEATURE: (A) NAME/KEY: intron (B) LOCATION: 4890..4967 (ix) FEATURE: (A) NAME/KEY: intron (B) LOCATION: 5295..5803 (ix) FEATURE: (A) NAME/KEY: intron (B) LOCATION: 6197..6339 (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 1: TCTAGATGAC GAAATCGCGC TACCTTTGAT TTNGAAATAC TAGGTTGTAG TATCTTGATT 60 AGTITTTTGG ATATCTTGCT GTAATTTCTT TAGGAGATGC AAACGGTCTT CATTTAATAT 120 GAGCCCTTGT GACTTGACAA AAGTATCTAG CATGTTTGAT CACGAGGTAG CTAAAAAGTA 180 GOJIGTTTGA TTAAGCACAT AATATTGTAT TGGGCCTATT GGCTATCAAT GAAGTTTGAT 240 GCAAGTATAT AGCTTGTATT ATGCATGTGA TGAGGGTATA TAAAAGAAGT AAAGAACATT 300 CICTCGTAGC ATTCATTTTT CTCΓTGCCTA TAGTTAACGA GΓITΓTGTCAC ACATGACGTT 360 GAAACTGGAT O'lUllTbTll' TTCCATCTAA GTTTGGATTA CCIGATAGAT GCTCAACTTC 420 TTΌSTCAGCC TTTΓCTTTCC GATTTTTCCC AAGACAAGAT TCΓΓTAGTTA ATAGTTATTG 480 CTCTGGTGGC TTGTGTGCAT TTTAGGAATC TTACTCTGTT TTTTAATGGA GAAACGAAAC 540 CTACCTTTTT ITLTLJIUI'IC CCTΓΓTATSA TATCACCTGC TTGGAGGCGT TTAGACTTTA 600 TCCACCTAAA CTATTCATGT TTACCAGACA AGCTATACGT TTTATCCCCC CCCCCCGCGG 660 ACCTGNGGAC AAAAGAAGOG CTGATGAACT GATITAATCC GTGTTTTATT ATATTACACA 720 TTGATGCTTC ATGGAGCTAA TATCTTTGGT TAAATTTCAT GTATATATAT ACCCTTCCCT 780 CTTGTGATGG CAGTGGCCCC TCGTTTAATT AGCGTACTTA ATTATCTGAT GGATACTGTA 840 TGCTTGGCAG ATGATGTCAT CAGATTATAC C.ATTTGTTGT GCTCTACAAA ATAAAAAACC 900 TCTATTTATG TTCATCTTTT TGGTAACAAG TAACTAATTG ATGCGCTATG TTGACAGGCG 960 ATGCATTACA CAACTTACGA ACTAGCTTGC AAGATCCCAA CAATXJTCCTG CAGAGCTGGG 1020 ATCCAACCCT TX7IGAACCCT TGCΛCATGGT TTCΑTGTGAC ATGTAACAAT GAAAACAGTG 1080 TTATAAGAGT GTAGGTCACT TCXrTTATTA ATTTTTTTAG C-AAGΓTTACGA ATATTTACTC 1140 AATTGAGCAG ATGTCTCTTT AAATATTTTT CTTTAATTTC TTAGCTAAGC GGAGCATCTA 1200 TCTTAAGTAT CTCTACTGAA TTTAAGACAT AATACATTTT TTTAAAAAAT CTATTAGAGT 1260 GTTITTTCCG CACAGCGCAC ATATATCTTT TTICTGGTAA TTCAGACAAC CTTTCTCCCG 1320 ACGATAAAAT AATATAAGAT TAACTCCTTG AACTAATTTT TTATITITCT TTTCTTTTTA 1380 TGTTCTTTGC AGAAAGTTTC TTATGGTCTT TTGTGAAAAG TACATTCTAT GATAATTΠT 1440 TGGCAACTCA TATAAATTTA TATATATTCC ATGTAGTTAT AAGTTAAAAA AAGCTTCCTA 1500 TTAATTCCAA GATAGAGGTT CATTTTTATA GTΓTGGGCAT CCΑTGAGTTT TTGAAAATGT 1560 CAGAAATTTT GTTGAGTTAA TTTTACTTAC CAACTITTAT GGCGTCATGC AGrKΛTCTTG 1620 GGAATGCAGC ATΓATCTGGT CAAITGGTTC CTCTTGGCCA GTTGAAAAAT TIACAATACT 1680 TGTAAGACCA TATCACTTGG AATGCTTTAG TTTTTATACA GCACAATGCT TTCAATATCT 1740 GTTAAAAGTG TGAAAAAGTT GACTTTCTAG CTTCAGCAGT TCTTCGGATA ATATCTATGA 1800 AGCACTTAAA AGGCTGGGCA ATTTΓΠTGT TATTATTTCA AATATTGTTA ATTGTTACTA I860 CTTAATATGA TAAACTGATT TAACTCCTCA TGATTGGTCT CΛGTCCAATG TGCCCTCATT 1920 AGTCACATNA TAAAATTGGN GGGTTGGACA AATATAACTT CTTTTCTTAA GGTCCAGAAA 1980 GAGCACTTAT C-AACCTTGTC TAGCGCATAA OSTCACAGTG QGTCAGTCAC GGGCTATCCA 2040 GTTTGGGGAG GTTTTAATGA GCACTTATΓT ACCTTGTCTT TTAAACGTCT GAGGATGTTA 2100 TTAAAGTCTG CATCATTCAG AGTTTAAATT AGCACTTTCA GTTGTATTAT GAATGGTACA 2160 TGAAAGATAC ATATCTTAAT GTTCCTATGC CTGTTTCAAC ATGTCTCTAA TATTCTGTTA 2220 TCITTGTCAT CTTAAAAATG GCACTGATTA AAATGTGAGA AAGGTAGTCT TCCAATACCA 2280 TTTCATGTAT ACCAGAGAAT ATCATAATTT TTTTAAATCA TAAGTTGGGC CCTAGAGTTT 2340 TCTCAGTATT GGTCTATTTA TATTTTCCAC CATTTAGAAC TGTGTTGTCA GATGAAAATC 2400 TTGGACTTCC ACAGAAGATC TTATAGTAAA AGTATTCTTT AGATCTGATG ATGAAAGTTG 2460 Tt-ATGGTGTG GCCTGTCCCA GAATTTAAAT OATCCCATG TCACATGTTT GTTGATCTGA 2520 CTACTCACTG TTAATCGAAG AGTAACTATT TGTGAATTAA ATGC'ITITIT Tl'rTUTllTr 2580 CATGCTTAGC GTTATAAAGG TCTACGTCTG ACTATGGTTT TTAACATGTT ATAGTTTTGT 2640 ACTGACAAGT TTAAAGTTTC TCTTGTTTAC GAATTAAGAA TATATAATAT AAAACGCTTT 2700 AACTITCTCT GTGGAAGGTG TTCTTACCTT TTTATATATA TATATAGATA CTX.AGACTCT 2760 GCTGGCAATT ATATCTTACG AACTTACGAG TATACAGAAC TTGTATATTA G3TTCAGATG 2820 AGIGGCTGTA GTAGAACACC TTAAGCAAGA ACT1_AATCAT GAGGrTTTCAA CCTTTTAACT 2880 TAG ATTTTTTCAA GTTTATGGAA AATTGTACCT CATGATCGTG σiTTCTTTCC 2940 ATAAACTTTC CATATAAGTC CXJITTCTTGA CGTTTTCATG TAAGCTGTTG ACGAGTGATT 3000 ATΓAGCGGTT CTTTCAATAA TCATAATGTG TX7ICACTTTG ATGAGGCCTG TACTTATTAT 3060 TGCACCTTGC ACTTAACCTT GATCCTCATG TCATCTTGAT TGTCATAGTC TACTAACCGA 3120 GrrrGAACATG GTTTATCATG TLTITIGAGG TAACAATGTA GCTTΓCACCT CTGTCCTTGA 3180 TATAGGΠTA AGGCTTGCAC CTCCCACTAG CCTITCGTTG TTITATTCAC AGTTCACACA 3240 CCTACTAGCA CTGrrTCACCT CTAGTCTTTT GTCOΞCAAAT AGTAAGAAGT TTCTΓΓCGCA 3300 TAATAGTGGA TCATCATTTA AGAAATAGTG AATCAAATTA TCGTGTTATT GTIGTTTGTAC 3360 TTTGGAATTA AATGAGTTGC TGAACATTGT TGCTGTTTAT CGTIUICAAG GCTTTGCCAA 3420 GGAAGGCGAT TAGTAAGAGT GGGCATCCAA GCGOCTTTAT CTTGAAGGGG CGGGCGGCAC 3480 GTTGTGGATT CTGGGTGTCT ATTAGAGGAC ATTATCTATA TATACTGATT ATTTATTAGA 3540 ATATAAATCA ACTACTATAT TTTTC.TTTGT AATGTTTATA TAGAAATCCC ACTCGTAAAC 3600 TTGACAAATA CCATTGAAAT ATTΓGAACCT AATTAATTAG TAGTGTCAGG TTTAAATTCA 3660 AACTCATTTA ATTTTACTTT AAAAAATAAT TCTATATGAA TCGTAACAGT ATAAATATAT 3720 TAAATTACAT GTATGTGTGC CTATATATAG CTGAATGTCT AATAGACTCC AAGACGGCTG 3780 CTCTTACTGC CTAGGCGTCC AGGCAGTTCA CTGATGCTTA CXTTGACAAA TATGGGGTTC 3840 GrrATGACATT GTTGGGGATC CCTATCACTG GATTCCTGTT TTGCTGACCC TCTGTTCAAT 3900 TGATTTTCAT TGATGTAGTA TTACTAGTTT TATAAATATT CTTTATTGCA ATAATTTAAC 3960 TGGAGTTTAA CAATGACAGG GAGCTTTACA GCAATAACAT AAGTGGACCA ATTCCTAGTG 4020 ATCTTGGGAA TCTGACAAAT TTGGTGAGCT TGGACCTATA CATGAATAGC TTCTCTGGAC 4080 CTATACCGGA CACATTAGGA AAGCTTACAA GGCTAAGATT CTTGTATGAC TACAAATCTT 4140 CACTAGTTTT TAACTTAATG CAATTTGATT ATΠTITTCAA GTGATTGATT ATATCACAAA 4200 TTACTGGATA GGCGTCTCAA CAACAACTGC CTCTCTGGTC CAATTCCAAT GTCACTGACT 4260 AATATTACAA CTCTTCAAGT CCTGTAAGTA TTOOSACCTT TCCAGATAGT TTTGTTGTTG 4320 TGGATGTTTC AATTTTAATA CTAAATATGT T^TCAGGGA TTTATCAAAC AATCGGCTAT 4380 CAGGACCAGT ACCGGATAAT GGCTCA.TTTT CmUHTAC ACCTATCAGG TTTAATGCTA 4440 GTAATATCTT TAATATTATG GTTCTTACTT CTACTGCGAA AGCTATGATA ATATTTTTTT 4500 TCTCCTTCAT ATATTATCAC TITCGCAGTT TTGGCAATAA TTTGAATTTA TCIGGACCTG 4560 TAACTGGGAG GαXTTGCCCT GGATCTCCCC CΑTTTTCTCC ACCACCTCCG TTCATCCCAC 4620 CATCAACAGT AC1AGCCTCCA GGTGATTTAG TTTTTATATT AAITCCCGTA ATTAATTTTA 4680 TGACTGTAAA AATTGGTGTT AATTTCACCA GTTGCGAATA AAGTATTTTC CTTCTTTCTC 4740 TTCTTATTAT TATGAAGGAC AAAATGGTCC CACTGGAGCT ATTGCTGGQG GAGTAGCTGC 4800 TGGTGCTGCT TTACTGTTTG CTCC-ACCTGC AATGGCATTT GCATGGTOGC GGAGAAGAAA 4860 ACCGCGAGAA CATTTCTTTG ATGTGCCAGG TTAGTCCTGT AAATAGATAT CTATTGAAGC 4920 GCTTACTGTC TGTGGACTTT GTITTCACTG TCATTAGTTA ACTTCAGCTG AAGAGGACCC 4980 AGAAGTGCAC CTTGGTCAAC TGAAGAGGTT TTCTCTGCGA GAATTGCAAG TCGCAACGGA 5040 TACTTTTAGT ACXΛTCCTTG GAAGAGGTGG ATTTGGTAAG GTGTATAAGG GACGCCTTGC 5100 TGKIGGCICA CTIGTAGCAG TTAAAAGGCT TAAAGAAGAA CGAACACCAG GTGGCGAGCT 5160 GCAGTTTCAA ACAGAAGTGG AAATGATTAG CATGGCTGTG CATCGAAATC TTCTGCGTCT 5220 ACGTGGTTTC TGCATGACAC CTACCGAGCG GCTTCTTGTA TATCCATACA TGGCTAATGG 5280 AAGTGTTGCG TCATGTTTAA GAGGTATCTC AGTTACAATT ACCATAACTT GCCAGAAGTT 5340 TGTTTGATTA AAAATGAAAT ATAACTCCCT ACACTATGTT AAGGTGTTAT AATTTCTGAG 5400 CAGATCTTAT TTCCCATTGC AAGATACCAG TTATTATTGT TTTTTCTGTA ATTGATACCG 5460 GTTATATTTC TTTCTTGTAT TTC^GTTATAT GCAAGGATTT CGAGTCTAAT AAGTTATCAA 5520 ACTGGATGCT ATGTTTATTC TGCAATTGAA TTCTTGCTTC ATGTGCCAAA ATATATATGA 5580 TTCAACTTGG AATCATCTTA TAATATACTG TCTAAAGTCA GCTGTTGACT TTCATCATTA 5640 ATTAGTCTTC ATAAATCAGA ATCTGCCTAG TGAGCTTTAC CGACATACTC TAAACCTTTC 5700 TTATGGCCCT GTATATAATC GTCCCACTTA CTTTATTCAG TTTX7ICTGCT CTCTGAATTT 5760 TTGATCTGTA C^TTGTGATG TUITGTTTTC ATCAAATGTA GACCGTCAGC CΛTCAGAACC 5820 TΠXCCTGAT TGGCCAACTA GGGAGAGGAT TXICACTAGGA TCTTCTAGGG GCCTATCTAA 5880 ATTGCATGAC CATTGTGATC CCAAGATTAT CCATCGCGAT GTAAAAGCTG CAAΛTATATT 5940 ATTGGACGAA GAATTTGAGG CTGTTGTAGG TGATTTTGGG TTAGCTAGGC TCATGGATTA 6000 CAAGGATACC CATGTTACGA CTGCTGTAAG GGGTACCATT GGGCACATAG CTCCCGAGTA 6060 CX^ICTCGACT GGAAAGTCAT CAGAGAAGAC CGATGTCTTT GGTTATGGGA TAATGCTCCT 6120 AGAGCTCATT ACTGGACAGA GGGCTTTTGA TCTTGCTCGC CTTGCGAACG ATGATGATGT 6180 TATGTTGTTG GATTGGGTAT CTOICCCGGG 'l^TlU-TriU GTTAATTATT TCACATATTA 6240 GTGCTTACTA CTTTGTTGTG GCCCTTTGTT TTTATTTCCT GCCTGTATTT GATTCTTAGT 6300 CATGTTATGC ATATTGACCT GCTTTGCAAT GTCTTTTAGG TTAAAAGCCT TTTGAAAGAG 6360 AAAAAGTTGG AGATGCTGGT OΞATCCTGAC CTGCAGAACA ATTACATTGA CACAGAAGTT 6420 GAGCAGCTTA TTCAAGTAGC ATTACTCTGT ACCCAGGGTT CGCCAATGGA GCGGCCTAAG 6480 ATGrrCAGAGG TAGTCCGAAT GCTTGAAGGT GATGGCCTTG CAGAAAAGTG GGACGAGTGG 6540 CAAAAAGTTG AAGTCATCCA TCAAGACGTA GAATTAGCTC CACATCGAAC TTCTGAATGG 6600 ATCCTAGACT CGACAGATAA CTTGCATGCT TTTGAATTAT CTGGTCCAAG ATAAACAGCA 6660 TATAAAATGT AATGAAATTA ATATTTTTTA TGGTT 6695 (2) INFORMATION FOR SEQ ID NO: 2: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1815 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: cDNA (iii) HYPOTHETICAL: NO (iii) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (A) ORGANISM: Daucus carota (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 94..1752 (Xi ) SEQUENCE DESCRIPTION: SEQ ID NO: 2 : GACAAATACC ATTGAAATAT TTGAACCTAA TTAATTAGTA GTGTCAGGTT TAAATTCAAA 60 CTCATTTAAT TTTACTTTAA AAAATAATTC TAT ATG AAT CGT AAC ACT ATA AAT 114 Met Asn Arg Asn Ser lie Asn 1 5 ATA TTA AAT TAC ATG CAG TTC ACT GAT GCT TAC CTT GAC AAA TAT GGG 162 He Leu Asn Tyr Met Gin Phe Thr Asp Ala Tyr Leu Asp Lys Tyr Gly 10 15 20 GTT CTT ATG ACA TTG GAG CTT TAC AGC AAT AAC ATA AGT GGA CCA ATT 210 Val Leu Met Thr Leu Glu Leu Tyr Ser Asn Asn He Ser Gly Pro He 25 30 35 CCT AGT GAT CTT GGG AAT CTG ACA AAT TTG GTG AGC TTG GAC CTA TAC 258 Pro Ser Asp Leu Gly Asn Leu Thr Asn Leu Val Ser Leu Asp Leu Tyr 40 45 50 55 ATG AAT AGC TTC TCT GGA CCT ATA CCG GAC ACA TTA GGA AAG CTT ACA 306 Met Asn Ser Phe Ser Gly Pro He Pro Asp Thr Leu Gly Lys Leu Thr 60 65 70 AGG CTA AGA TTC TTG CGT CTC AAC AAC AAC AGC CTC TCT GGT CCA ATT 354 Arg Leu Arg Phe Leu Arg Leu Asn Asn Asn Ser Leu Ser Gly Pro He 75 80 85 CCA ATG TCA CTG ACT AAT ATT ACA ACT CTT CAA GTC CTG GAT TTA TCA 402 Pro Met Ser Leu Thr Asn He Thr Thr Leu Gin Val Leu Asp Leu Ser 90 95 100 AAC AAT CGG CTA TCA GGA CCA GTA CCG GAT AAT GGC TCA TTT TCT TTG 450 Asn Asn Arg Leu Ser Gly Pro Val Pro Asp Asn Gly Ser Phe Ser Leu 105 110 115 TTT ACA CCT ATC ACT TTT GCC AAT AAT TTG AAT TTA TGT GGA CCC GTA 498 Phe Thr Pro He Ser Phe Ala Asn Asn Leu Asn Leu Cys Gly Pro Val 120 125 130 135 ACT GGG AGG CCC TGC CCT GGA TCT CCC CCA TTT TCG CCA CCA CCT CCG 546 Thr Gly Arg Pro Cys Pro Gly Ser Pro Pro Phe Ser Pro Pro Pro Pro 140 145 150 TTC ATC CCA CCA TCA ACA GTA CAG CCT CCA GGA CAA AAT GGT CCC ACT 594 Phe He Pro Pro Ser Thr Val Gin Pro Pro Gly Gin Asn Gly Pro Thr 155 160 165 GGA GCT ATT GCT GGG GGA CTA GCT GCT GCT GCT GCT TTA CTG TTT GCT 642 Gly Ala He Ala Gly Gly Val Ala Ala Gly Ala Ala Leu Leu Phe Ala 170 175 180 GCA CCT GCA ATG GCA TTT GCA TGG TGG CGG AGA AGA AAA CCG CGA GAA 690 Ala Pro Ala Met Ala Phe Ala Trp Trp Arg Arg Arg Lys Pro Arg Glu 185 190 195 CAT TTC TTT GAT GTG CCA GCT GAA GAG GAC CCA GAA GTG CAC CTT GGT 738 His Phe Phe Asp Val Pro Ala Glu Glu Asp Pro Glu Val His Leu Gly 200 205 210 215 CAA CTG AAG AGG TTT TCT CTG CGA GAA TTG CAA GTC GCA ACG GAT ACT 786 Gin Leu Lys Arg Phe Ser Leu Arg Glu Leu Gin Val Ala Thr Asp Thr 220 225 230 TTT AGT ACC ATA CTT GGA AGA GGT GGA TTT GGT AAG GTG TAT AAG GGA 834 Phe Ser Thr He Leu Gly Arg Gly Gly Phe Gly Lys Val Tyr Lys Gly 235 240 245 CGC CTT GCT GAT GGC TCA CTT GTA GCA GTT AAA AGG CTT AAA GAA GAA 882 Arg Leu Ala Asp Gly Ser Leu Val Ala Val Lys Arg Leu Lys Glu Glu 250 255 260 CGA ACA CCA GCT GGT GAG CTG CAG TTT CAA ACA GAG GTG GAA ATG ATT 930 Arg Thr Pro Gly Gly Glu Leu Gin Phe Gin Thr Glu Val Glu Met He 265 270 275 AGC ATG GCT GTG CAT CGA AAT CTT CTG OCT CTA CCT GGT TTC TGC ATG 978 Ser Met Ala Val His Arg Asn Leu Leu Arg Leu Arg Gly Phe Cys Met 280 285 290 295 ACA CCA ACA GAG CGG CTT CTT GTA TAT CCA TAC ATG GCT AAT GGA AGT 1026 Thr Pro Thr Glu Arg Leu Leu Val Tyr Pro Tyr Met Ala Asn Gly Ser 300 305 310 GTT GCG TCG TCT TTA AGA GAG CCT CAG CCA TCA GAA CCT CCC CTT GAT 1074 Val Ala Ser Cys Leu Arg Glu Arg Gin Pro Ser Glu Pro Pro Leu Asp 315 320 325 TGG CCA ACT AGG AAG AGG ATT GCA CTA GGA TCT GCT AGG GGG CTT TCT 1122 Trp Pro Thr Arg Lys Arg He Ala Leu Gly Ser Ala Arg Gly Leu Ser 330 335 340 TAT TTG CAT GAC CAT TGT GAT CCC AAG ATT ATC CAT CGT GAT GTA AAA 1170 Tyr Leu His Asp His Cys Asp Pro Lys He He His Arg Asp Val Lys 345 350 355 GCT GCA AAT ATA TTA TTG GAC GAA GAA TTT GAG GCT GTT GTA GGT GAT 1218 Ala Ala Asn He Leu Leu Asp Glu Glu Phe Glu Ala Val Val Gly Asp 360 365 370 375 TTT GGG TTA GCT AGG CTC ATG GAT TAC AAG GAT ACC CAT GTT ACA ACT 1266 Phe Gly Leu Ala Arg Leu Met Asp Tyr Lys Asp Thr His Val Thr Thr 380 385 390 GCT GTA AGG GGT ACC TTG GGC TAC ATA GCT CCC GAG TAC CTC TCG ACT 1314 Ala Val Arg Gly Thr Leu Gly Tyr He Ala Pro Glu Tyr Leu Ser Thr 395 400 405 GGA AAG TCA TCA GAG AAG ACC GAT GTC TTT GGT TAT GGG ATT ATG CTC 1362 Gly Lys Ser Ser Glu Lys Thr Asp Val Phe Gly Tyr Gly He Met Leu 410 415 420 TTA GAG CTC ATT ACT GGA CAG AGA GCT TTT GAT CTT GCT CGC CTT GCG 1410 Leu Glu Leu He Thr Gly Gin Arg Ala Phe Asp Leu Ala Arg Leu Ala 425 430 435 AAC GAT GAT GAT GTT ATG TTG TTG GAT TGG GTT AAA AGC CTT TTG AAA 1458 Asn Asp Asp Asp Val Met Leu Leu Asp Trp Val Lys Ser Leu Leu Lys 440 445 450 455 GAG AAA AAG TTG GAG ATG CTG GTC GAT CCT GAC CTG GAG AAC AAT TAC 1506 Glu Lys Lys Leu Glu Met Leu Val Asp Pro Asp Leu Glu Asn Asn Tyr 460 465 470 ATT GAC ACA GAA GTT GAG CAG CTT ATT CAA GTA GCA TTA CTC TGT ACC 1554 He Asp Thr Glu Val Glu Gin Leu He Gin Val Ala Leu Leu Cys Thr 475 480 485 CAG GGT TCG CCA ATG GAG CGG CCT AAG ATG TCA GAG CTA GTC CGA ATG 1602 Gin Gly Ser Pro Met Glu Arg Pro Lys Met Ser Glu Val Val Arg Met 490 495 500 CTT GAA GCT GAT GGC CTT GCA GAA AAG TGG GAC GAG TGG CAA AAA GTA 1650 Leu Glu Gly Asp Gly Leu Ala Glu Lys Trp Asp Glu Trp Gin Lys Val 505 510 515 GAA GTC ATC CAT CAA GAC GTA GAA TTA GCT CCA CAT CGA ACT TCT GAA 1698 Glu Val He His Gin Asp Val Glu Leu Ala Pro His Arg Thr Ser Glu 520 525 530 535 TGG ATC CTA GAC TCG ACA GAT AAC TTG CAT GCT TTT GAA TTA TCT GCT 1746 Trp He Leu Asp Ser Thr Asp Asn Leu His Ala Phe Glu Leu Ser Gly 540 545 550 CCA AGA TAAACAGCAT ATAAAATGTG AATGAAATTA ATATTTTTTA TGGTTAAAAA 1802 Pro Arg AAAAAAAAAA AAA 1815 (2) ΓNFORMATTON FOR SEQ ID NO: 3: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 553 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 3: Met Asn Arg Asn Ser He Asn He Leu Asn Tyr Met Gin Phe Thr Asp 1 5 10 15 Ala Tyr Leu Asp Lys Tyr Gly Val Leu Met Thr Leu Glu Leu Tyr Ser 20 25 30 Asn Asn He Ser Gly Pro He Pro Ser Asp Leu Gly Asn Leu Thr Asn 35 40 45 Leu Val Ser Leu Asp Leu Tyr Met Asn Ser Phe Ser Gly Pro He Pro 50 55 60 Asp Thr Leu Gly Lys Leu Thr Arg Leu Arg Phe Leu Arg Leu Asn Asn 65 70 75 80 Asn Ser Leu Ser Gly Pro He Pro Met Ser Leu Thr Asn He Thr Thr 85 90 95 Leu Gin Val Leu Asp Leu Ser Asn Asn Arg Leu Ser Gly Pro Val Pro 100 105 110 Asp Asn Gly Ser Phe Ser Leu Phe Thr Pro He Ser Phe Ala Asn Asn 115 120 125 Leu Asn Leu Cys Gly Pro Val Thr Gly Arg Pro Cys Pro Gly Ser Pro 130 135 140 Pro Phe Ser Pro Pro Pro Pro Phe He Pro Pro Ser Thr Val Gin Pro 145 150 155 160 Pro Gly Gin Asn Gly Pro Thr Gly Ala He Ala Gly Gly Val Ala Ala 165 170 175 Gly Ala Ala Leu Leu Phe Ala Ala Pro Ala Met Ala Phe Ala Trp Trp 180 185 190 Arg Arg Arg Lys Pro Arg Glu His Phe Phe Asp Val Pro Ala Glu Glu 195 200 205 Asp Pro Glu Val His Leu Gly Gin Leu Lys Arg Phe Ser Leu Arg Glu 210 215 220 Leu Gin Val Ala Thr Asp Thr Phe Ser Thr He Leu Gly Arg Gly Gly 225 230 235 240 Phe Gly Lys Val Tyr Lys Gly Arg Leu Ala Asp Gly Ser Leu Val Ala 245 250 255 Val Lys Arg Leu Lys Glu Glu Arg Thr Pro Gly Gly Glu Leu Gin Phe 260 265 270 Gin Thr Glu Val Glu Met He Ser Met Ala Val His Arg Asn Leu Leu 275 280 285 Arg Leu Arg Gly Phe Cys Met Thr Pro Thr Glu Arg Leu Leu Val Tyr 290 295 300 Pro Tyr Met Ala Asn Gly Ser Val Ala Ser Cys Leu Arg Glu Arg Gin 305 310 315 320 Pro Ser Glu Pro Pro Leu Asp Trp Pro Thr Arg Lys Arg He Ala Leu 325 330 335 Gly Ser Ala Arg Gly Leu Ser Tyr Leu His Asp His Cys Asp Pro Lys 340 345 350 He He His Arg Asp Val Lys Ala Ala Asn He Leu Leu Asp Glu Glu 355 360 365 Phe Glu Ala Val Val Gly Asp Phe Gly Leu Ala Arg Leu Met Asp Tyr 370 375 380 Lys Asp Thr His Val Thr Thr Ala Val Arg Gly Thr Leu Gly Tyr He 385 390 395 400 Ala Pro Glu Tyr Leu Ser Thr Gly Lys Ser Ser Glu Lys Thr Asp Val 405 410 415 Phe Gly Tyr Gly He Met Leu Leu Glu Leu He Thr Gly Gin Arg Ala 420 425 430 Phe Asp Leu Ala Arg Leu Ala Asn Asp Asp Asp Val Met Leu Leu Asp 435 440 445 Trp Val Lys Ser Leu Leu Lys Glu Lys Lys Leu Glu Met Leu Val Asp 450 455 460 Pro Asp Leu Glu Asn Asn Tyr He Asp Thr Glu Val Glu Gin Leu He 465 470 475 480 Gin Val Ala Leu Leu Cys Thr Gin Gly Ser Pro Met Glu Arg Pro Lys 485 490 495 Met Ser Glu Val Val Arg Met Leu Glu Gly Asp Gly Leu Ala Glu Lys 500 505 510 Trp Asp Glu Trp Gin Lys Val Glu Val He His Gin Asp Val Glu Leu 515 520 525 Ala Pro His Arg Thr Ser Glu Trp He Leu Asp Ser Thr Asp Asn Leu 530 535 540 His Ala Phe Glu Leu Ser Gly Pro Arg 545 550 (2) INFORMATION FOR SEQ ID NO: 4: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 13 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: unknown (iii) HYPOTHETICAL: NO (iii) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (A) ORGANISM: primer (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 4: TTTTTTTTTT TGC 13 (2) INFORMATION FOR SEQ ID NO: 5: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 10 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: unknown (iii) HYPOTHETICAL: NO (iii) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (A) ORGANISM: primer (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 5: GGGATCTAAG 10 (2) INFORMATION FOR SEQ ID NO: 6: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 10 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: unknown (iii) HYPOTHETICAL: NO (iii) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (A) ORGANISM: primer (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 6: ACACGTGGTC 10 (2) INFORMATION FOR SEQ ID NO: 7: (i) SEQUENCE C.HARACTERIΞTICS: (A) LENGTH: 10 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: unknown (iii) HYPOTHETICAL: NO (iii) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (A) ORGANISM: primer (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 7: TX^ΞCACAGG 10 (2) INFORMATTCN FOR SEQ ID NO: 8: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 14 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: unknown ( iii ) HYPOTHETICAL: NO (iii ) ANTI-SENSE: NO (vi ) ORIGINAL SOURCE: (A) ORGANISM: primer (XI) SEQUENCE DESCRIPTION: SEQ ID NO: 8: TΓITITITIT TCTG 14 (2) INFORMATION FOR SEQ ID NO: 9: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 13 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: unknown (iii) HYPOTHETICAL: NO (iii) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (A) ORGANISM: primer (xi) SEQUENCE DESCRIPTICiN: SEQ ID NO: 9: '1T1T1T1T1T TCA 13 (2) INPORMATION FOR SEQ ID NO: 10: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 10 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: unknown (iii) HYPOTHETICAL: NO (iii) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (A) ORGANISM: primer (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 10: GACATCGTCC 10 (2) INFORMATION FOR SEQ ID NO: 11: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 10 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: unknown (iii) HYPOTHETICAL: NO (iii) ANTT-SENSE: NO (vi) ORIGINAL SOURCE: (A) ORGANISM: primer (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 11: CCCTACTGGT 10 (2) INFORMATION FOR SEQ ID NO: 12: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 10 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: unknown (iii) HYPOTHETICAL: NO (iii) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (A) ORGANISM: primer (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 12: ACACGTGGTC 10 (2) INFORMATION FOR SEQ ID NO: 13: (i) SEQUENCE CHARACTERISTICS: (A) I-ENGTH: 10 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS : single (D) TOPOLOGY: unknown (iii) HYPOTHETICAL: NO (iii) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (A) ORGANISM: primer (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 13: GGTGACTGTC 10 (2) INFORMATION FOR SEQ ID NO: 14: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 18 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: unknown (iii) HYPOTHETICAL: NO (iii) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (A) ORGANISM: primer (xi) SEQUENCE DESCRIPTION: SBQ ID NO: 14: TCTTGGACCA GATAATTC 18 (2) INFORMATION FOR SEQ ID NO: 15: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 19 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: unknown (iii) HYPOTHETICAL: NO (iii) ANTI-SENSE: ND (vi) ORIGINAL SOURCE: (A) ORGANISM: primer (xi) SEQUENCE DESCRIPTION: SBQ ID NO: 15: CTCTGATGAC TTTCCAGTC 19 (2) INFORMATION FOR SBQ ID NO: 16: (i) SEQUENCE CHARACTERISTICS: (A) IJENGTH: 16 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: unknown (iii) HYPOTHETICAL: NO (iii) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (A) ORGANISM: primer (xi) SEQUENCE DESCRIPTTON: SBQ ID NO: 16: AATGGCATTT GCATGG 16 (2) INFCfRMATTON FOR SBQ TD NO: 17: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 5 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iii) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (A) ORGANISM: Daucus carota (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 17: Ser Pro Pro Pro Pro 1 5 (2) INFORMATION FOR SBQ ID NO: 18: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 8 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iii) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (A) ORGANISM: Daucus carota (xi) SEQUENCE DESCRIPTION: SEQ ID ND: 18: His Arg Asp Val Lys Ala Ala Asn (2) INFORMATION FOR SEQ ID NO: 19: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 9 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: single (D) TOPOLOGY: unknown (ii) MOLECULE TYPE: peptide (iii) HYPOTHETICAL: NO (iii) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (A) ORGANISM: Daucus carota (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 19: Gly Thr Leu Gly Tyr He Ala Pro Glu 1 5 (2) INFORMATION FOR SEQ ID NO: 20: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 4081 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: DNA (genomic) (iii) HYPOTHETICAL: NO (vi) ORIGINAL SOURCE: (A) ORGANISM: Arabidopsis thaliana (vii) IMMEDIATE SOURCE: (B) CLONE: Arabidopsis SERK gene (ix) FEATURE: (A) NAME/KEY: exon (B) LOCATION: 1280..1367 (ix) FEATURE: (A) NAME/KEY: exon (B) LOCATION: 1796..1928 (ix) FEATURE: (A) NAME/KEY: exon (B) LOCATION: 2014..2085 (ix) FEATURE: (A) NAME/KEY: exon (B) LOCATION: 2203..2346 (ix) FEATURE: (A) NAME/KEY: exon (B) LOCATION: 2450..2521 (ix) FEATURE: (A) NAME/KEY: exon (B) LOCATION: 2617..2688 (ix) FEATURE: (A) NAME/KEY: exon (B) LOCATION: 2772.-2884 (ix) FEATURE: (A) NAME/KEY: exon (B) LOCATION: 3015..3146 (ix) FEATURE: (A) NAME/KEY: exon (B) LOCATTCN: 3305..3646 (ix) FEATURE: (A) NAME/KEY: exon (B) LOCATION: 3760. .4081 (xi ) SEQUENCE DESCRIPTION: SBQ ID NO: 20 : TCTAGAAACC TTTTGATCAT AATGAAAATA AAGAGTCCAT CTACCACATG GGGTAAGCAT 60 AATGTGTGAT ATTTAAAGGG TAACAAATGT AATCTGCTTT TTATTTTACT TTTTACCTCT 120 ACTCAAATTG TATGOGCAGT T'l'l'l'l'lTlTl' TTTTAAATGA TAAGACAACT ATCTGTTTAA 180 TGCTATTGTG ATGAAACAGT ACTAAAGTCA TATCGGGCAC GCCATACTAC TTCCACAGTG 240 GAACTTGGCC AAATTTTGTC TTTGCCGTCT CTACAGTTTC TTCCACCAAA TTTTITGTTG 300 ACAAAACTCA AATCTTTCAA TCTCATCTCT GCCAAAGTTG GGTTTAGAAA GAATATCAGC 360 AAACACTAAT ATCTTTATTG TTCXΛTGGTT TATCAATCAC AAAATTCACA ACCATTGTAA 420 AAAAAAATTC ACATTTTTGG TATGAGATTG CrCACATGAT AGTGAACCTC TTTAACATTT 480 TAACTTTACT TTCATAAATA O.CXΪATTACG AATCTTACTT GCATTAAAAA TTTAGAAAAG 540 GTTTTTCTAC TTAAAGAAAA AAGGGACCCA ACAGAGAGAG GITTGACCAG GAGAAACGGG 600 TC<-ATAGCCT TAAGAGCTTT CLAACTACTTT ACCCCAAACC CAAAGCGATG TCACTTTCAA 660 CCATCTCTTC TCTCCCCCGA ACCCGTTTTT TTGAlCCGGTC AGTTCGGGCA GCAGCACCGT 720 TACGGGCAGC TTATATTCCT CCTVl'lCCTC CTCTACACCA CTGCATGCCC ATAAATAAAG 780 CCCGTTGAGA TCTTTAAAAA TATTAAATAA TATATCAACG AAAAAGCTAT TITATTCATA 840 AGAAGAAAAA GAGAGGAACA ACAACAACAC ACTAATCATA GTTICTCTGG CΛGOCTTCTT 900 GTIGCGGCTT AATAAAAAGC TCTTTTGTTA TTATTACTTC ACGTAGATTT TCCCCAAAAA 960 CKTCTTATTT TTITGTTTAA AAAAAAAACT TICATCTTTA TTCAACl'l'lT GTITTTACAGT 1020 CmSTGTGTGA GAGAGAGAGT CTGGTTTGAT TGAGGAAAGA CGACGACGAG AACGCCGGAG 1080 AATTAGGATT TTTATTTTAT TTITTACTCT TTGTTTGTTT TAATGCTAAT GGGTITrTAA 1140 AAGGGTTATC GAAAAAATGA CTGAGITTGT GTTGAGGTTG TCTCTCTAAA GTGTTAATGG 1200 TGGTGATTTT CGGAAGTTAG GGTTTΓCTCG GATCTGAAGA GATCAAATCA AGATTCGAAA 1260 TTTAGCATTG TTGTTTGAAA TGGAGTCGAG TTATGTGGTG TTTATCTTAC TTICACTGAT 1320 CTTACTTCCG AATCATTCAC TGTGGCTTGC TTCTGCTAAT TTGGAAGGTT CGTGGTTACT 1380 CAATTACTCA GCTTTACTCG TTTCTCAATT ACTITCTCGA TTCTTTTTTA TTTGGAGGTG 1440 AATCGCTATC TTTACTGTCT GCATTITGAT TTATGAAAAT TGTTGTTGTT CTTTGTATTT 1500 GTAAGATTTA GTGGCTAGTA CTTTGAATAC ACTCrTTTTGC TTl'll'lTGTT CAGATCAACT 1560 TTCTATATTG TAAAGGCATG TTCTITGGGT TGAAAAGCTG GGTTATTTGA TATCTTAAGA 1620 TTC4ATGTTGT TGATCCAAAC ATTCTCTGAA AGACTTCATT TGTITTTTGCT TTTCTAAAGA 1680 ATITCTTTAA TTATTAGCCT CTAATCTCAG AGAGGCCTGT TTGAATAGTT CTCTCTTGAA 1740 ATTAGACTTT TCACCAATTG ATGCTAATTG TGTAGATTTG TTGTTCTTCT TATAGGTGAT 1800 GCTITGCATA CTTTGAGGGT TACTCTACTT GATCCAAACA ATGTCTTGCA GAGCTGGGAT 1860 CCTACGCTAG TGAATCCTTG CACATGGTTC CΛTGTCACTT GCaACAACGA GAACAGTGTC 1920 ATAAGAGTGT AAAGCTTTCT TCTACTAATC CCAL'l'lTlTA AACTTTGACC TCAGCGTGCT 1980 TACCGACATT TTTCTTTCTT TTGTCAAATA CAGTGATTTG GGGAATGCAG AGTTATCTGG 2040 CCATTTAGTT CCAGAGCTTG GTOIGCTCAA GAATTTGCAG TAITTGTAAG TTCCACTTAT 2100 GCATCATGCT TTAACAAAAC AAATCCAAGA TTTGACAGAA GAAGCACTGG AGTTACCTTT 2160 TCTAATTGAA ATCTTTTTAA CAAGTTTCTT ATTTTCTTAC AQGGAGCTTT ACACTAACAA 2220 CATAACTGGC CCGATTCCTA CTAATCTTGG AAATCTGACA AACTTAGTGA GTTTGGATCT 2280 TTACTTAAAC ACTTTCTCCG GTCCTATTCC CSGAATCATTG GGAAAGCTTT CAAAαTTGAG 2340 ATTTCTGTGA CTATACATAT GCTTTACCGG CTCAGTTACA GTCTITGTTT AATCTTAGGT 2400 TTTGTTCCAA TTTTTGACTC TTTGCTGAAA ATTTTACATG CAAGAATAGC CGGCTTAACA 2460 ACAAC-AGTCT CACTGGGTCA ATTCCTATCT CACTGACCAA TATTACTACC CTTCAAGTGT 2520 TGTGAGTCCT CTCATTAACT TTCATTTATG TCTACTTCAT TCTCCCTCAG TTGATT1U1T 2580 GAGTTAATGC ACTTAACCTT GATGGATGCA ACACAGAGAT CTATCAAATA ACAGACTCTC 2640 TGGTTCAGTT CCTGACAATG GCTCCTTCTC ACTCTTCACA CCCATCAGGT TCTATGATTT 2700 ATCCTCTTCA GTTATTTCAG TTCXTGTGTC AGTGTCTGAA CTTATTCTGA AACTTTCATT 2760 TCCTTCTGCA GITTTGCTAA TAACTTAGAC CTATGTGGAC CTGTTACAAG TCACCCATCT 2820 CCTGGATCTC CCCCGTTTTC TCCTCCACCA CCTTTTATTC AACCTCCCCC AGTTTCCACC 2880 CCGAGTAAGC CTCCTCTTTT TAGTTTACAT TATAGGAAAC AGAAGATGAA ATCTTTGCTT 2940 CTCTGTCAAT CCTITΓΓCTC ATATAACTCA TCTTGCCAAT AAGGCAATAA CCAAATGATC 3000 TAATTTGATT TCAGGTGGGT ATGGTATAAC TGGAGCAATA GCTGGTGGAG TTGCTGCAGG 3060 TGCTGCTTTG CTCTTTGCTG CTCCTGCAAT AGCCTTTGCT TGGTGGCGAC GAAGAAAGCC 3120 ACTAGATATT TTCTTCGATG TGCXTGGTGA GTTTATTATT CGCATTAGTT TCTGTTCTTA 3180 C^CCAGCAATT TIUI'ITIUCA GAAAAGTATT CXW^CAACTG TTAATGAAAA TCAATACATA 3240 AGTCATTGTT TTTTAAGTTA CAAACTCTTT TGACTAAAAT CTCGATTGCA AAATCTCTAT 3300 GCAGCCGAAG AAGATCCAGA AGITCATCTG GGACAGCTCA AGAGGTTTTC TTTGCGGGAG 3360 CTACAAGTGG CGAGTGATGG GTTTAGTAAC AAGAACATTT TGGGCAGAGG TGGGTTTGGG 3420 AAAGTCTACA AGGGACGCTT GCO^GACGGA ACTCTTGTTG CTCTCAAGAG ACTGAAGGAA 3480 GAGCGAACTC C.AGGTGGAGA GCTCCAGTTT CAAACAGAAG TAGAGATGAT AACTATGGCA 3540 GTTCATCGAA ACCTGTTGAG ATTACGAGGT TTCTGTATGA CACCGACCGA GAGATTGCTT 3600 GΓGTATCCTT ACATGGCCAA TΌGAAGTGTT CXTTCGTGTC TCAGAGGTAA AAACTAAACA 3660 ATTAAACATC TTGTGCTCTC TCTCAATTAC TTTGACGTGA AGTGTTTTTT CATGTTTTCC 3720 TTTATGGGTT CATAATTGTT GGTTACACTA ATGACACAGA GAGGCCACCG TCACAACCTC 3780 CGCTTGATTG GCCAACGCGG AAGAGAATCG CGCTAGGCTC AGCTCGAGCT TTGTCTTACC 3840 TACATGATCA CTGCGATCCG AAGATCATTC ACCGTGACCT AAAAGCAGCA AACΛTCCTCT 3900 TAGACGAAGA ATTCGAAGCG GTTGTTGGAG ATITCGGGTT GGCAAAGCTA ATO-ACTATA 3960 AAGACACTCA O-TG-ACAACA GCA&TCCGriG GCMXΑTCGG TCACATCGCT CCAGAATATC 4020 TCTCAACCGG AAAATCTTCA GAGAAAACCG ACGTTTTCGG AT3\CGGAATC ATGCTTCTAG 4080 A 4081 - 68 - (2) INFORMATION FOR SEQ ID NO: 21: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 494 amino acids (B) TYPE: amino acid (C) STRANDEDNESS: unknown (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (iii) HYPOTHETICAL: NO (v) FRAGMENT TYPE: N-terminal (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 21: Met Glu Ser Ser Tyr Val Val Phe He Leu Leu Ser Leu He Leu Leu 1 5 10 15 Pro Asn His Ser Leu Trp Leu Ala Ser Ala Asn Leu Glu Gly Asp Ala 20 25 30 Leu His Thr Leu Arg Val Thr Leu Val Asp Pro Asn Asn Val Leu Gin 35 40 45 Ser Trp Asp Pro Thr Leu Val Asn Pro Cys Thr Trp Phe His Val Thr 50 55 60 Cys Asn Asn Glu Asn Ser Val He Arg Val Asp Leu Gly Asn Ala Glu 65 70 75 80 Leu Ser Gly His Leu Val Pro Glu Leu Gly Val Leu Lys Asn Leu Gin 85 90 95 Glu Leu Tyr Ser Asn Asn He Thr Gly Pro He Pro Ser Asn Leu Gly 100 105 110 Asn Leu Thr Asn Leu Val Ser Leu Asp Leu Tyr Leu Asn Ser Phe Ser 115 120 125 Gly Pro He Pro Glu Ser Leu Gly Lys Leu Ser Lys Leu Arg Phe Leu 130 135 140 Arg Leu Asn Asn Asn Ser Leu Thr Gly Ser He Pro Met Ser Leu Thr 145 150 155 160 Asn He Thr Thr Leu Gin Val Leu Asp Leu Ser Asn Asn Arg Leu Ser 165 170 175 Gly Ser Val Pro Asp Asn Gly Ser Phe Ser Leu Phe Thr Pro He Ser 180 185 190 Phe Ala Asn Asn Leu Asp Leu Cys Gly Pro Val Thr Ser His Pro Cys 195 200 205 Pro Gly Ser Pro Pro Phe Ser Pro Pro Pro Pro Phe He Gin Pro Pro 210 215 220 Pro Val Ser Thr Pro Ser Gly Tyr Gly He Thr Gly Ala He Ala Gly 225 230 235 240 Gly Val Ala Ala Gly Ala Ala Leu Leu Phe Ala Ala Pro Ala He Ala 245 250 255 Phe Ala Trp Trp Arg Arg Arg Lys Pro Leu Asp He Phe Phe Asp Val 260 265 270 Pro Ala Glu Glu Asp Pro Glu Val His Leu Gly Gin Leu Lys Arg Phe 275 280 285 Ser Leu Arg Glu Leu Gin Val Ala Ser Asp Gly Phe Ser Asn Lys Asn 290 295 300 He Leu Gly Arg Gly Gly |Phe Gly Lys Val Tyr Lys Gly Arg Leu Ala 305 310 \ 315 320 Asp Gly Thr Leu Val Ala Val Lys Arg Leu Lys Glu Glu Arg Thr Pro 325 330 335 Gly Gly Glu Leu Gin Phe Gin Thr Glu Val Glu Met He Ser Met Ala 340 345 350 Val His Arg Asn Leu Leu Arg Leu Arg Gly Phe Cys Met Thr Pro Thr 355 360 365 Glu Arg Leu Leu Val Tyr Pro Tyr Met Ala Asn Gly Ser Val Ala Ser 370 375 380 Cys Leu Arg Glu Arg Pro Pro Ser Gin Pro Pro Leu Asp Trp Pro Thr 385 390 395 400 Arg Lys Arg He Ala Leu Gly Ser Ala Arg Gly Leu Ser Tyr Leu His 405 410 415 Asp His Cys Asp Pro Lys He He His Arg Asp Val Lys Ala Ala Asn 420 425 430 He Leu Leu Asp Glu Glu Phe Glu Ala Val Val Gly Asp Phe Gly Leu 435 440 445 Ala Lys Leu Met Asp Tyr Lys Asp Thr His Val Thr Thr Ala Val Arg 450 455 460 Gly Thr He Gly His He Ala Pro Glu Tyr Leu Ser Thr Gly Lys Ser 465 470 475 480 Ser Glu Lys Thr Asp Val Phe Gly Tyr Gly He Met Leu Leu 485 490 (2) INFORMATION FOR SEQ ID NO: 22: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 1106 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: cDNA to mRNA (iii) HYPOTHETICAL: NO (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 142..795 (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 22: TCGACCCACG CGTCCGTCCA ACTTCAATAA AGGGGAAACC AACCTAACCC TAATTTTGCT 60 TTCTCCTCTT TGTTCAGAAA ATTTTCCCTT TACTCTCAAA TTCCTTTTCG ATTTCCCTCT 120 CTTAAACCTC CGAAAGCTCA C ATG GCG TCT CGA AAC TAT CGG TGG GAG CTC 171 Met Ala Ser Arg Asn Tyr Arg Trp Glu Leu 1 5 10 TTC GCA GCT TCG TTA ACC CTA ACC TTA GCT TTG ATT CAC CTG GTC GAA 219 Phe Ala Ala Ser Leu Thr Leu Thr Leu Ala Leu He His Leu Val Glu 15 20 25 GCA AAC TCC GAA GGA GAT GCT CTC TAC GCT CTT CGC CGG AGT TTG ACA 267 Ala Asn Ser Glu Gly Asp Ala Leu Tyr Ala Leu Arg Arg Ser Leu Thr 30 35 40 GAT CCA GAC CAT GTC CTC CAG AGC TGG GAT CCA ACT CTT GTT AAT CCT 315 Asp Pro Asp His Val Leu Gin Ser Trp Asp Pro Thr Leu Val Asn Pro 45 50 55 TGT ACC TGG TTC CAT GTC ACC TCT AAC CAA GAC AAC CGC GTC ACT CGT 363 Cys Thr Trp Phe His Val Thr Cys Asn Gin Asp Asn Arg Val Thr Arg 60 65 70 GTG GAT TTG GGA AAT TCA AAC CTC TCT GGA CAT CTT GCG CCT GAG CTT 411 Val Asp Leu Gly Asn Ser Asn Leu Ser Gly His Leu Ala Pro Glu Leu 75 80 85 90 GGG AAG CTT GAA CAT TTA CAG TAT CTA GAG CTC TAC AAA AAC AAC ATC 459 Gly Lys Leu Glu His Leu Gin Tyr Leu Glu Leu Tyr Lys Asn Asn He 95 100 105 CAA GGA ACT ATA CCT TCC GAA CTT GGA AAT CTG AAG AAT CTC ATC AGC 507 Gin Gly Thr He Pro Ser Glu Leu Gly Asn Leu Lys Asn Leu He Ser 110 115 120 TTG GAT CTG TAC AAC AAC AAT CTT ACA GGG ATA GTT CCC ACT TTC TTG 555 Leu Asp Leu Tyr Asn Asn Asn Leu Thr Gly He Val Pro Thr Phe Leu 125 130 135 GGA AAA TTG AAG TCT CTG GTC TTT TTA CGG CTT AAT GAC AAC CGA TTG 603 Gly Lys Leu Lys Ser Leu Val Phe Leu Arg Leu Asn Asp Asn Arg Leu 140 145 150 ACC GCT CCA ATC CTA GAG CAC TCA CGG CAA TCC CAA GCC TTT AAA GTT 651 Thr Gly Pro He Leu Glu His Ser Arg Gin Ser Gin Ala Phe Lys Val 155 160 165 170 GTT GAC GTC TCA AGC AAT GAT TTG TGT GGG ACA ATC CCA ACA AAC GGA 699 Val Asp Val Ser Ser Asn Asp Leu Cys Gly Thr He Pro Thr Asn Gly 175 180 185 CCC TTT GCT CAC ATT CCT TTA CAG AAC TTT GAG AAC AAC CCG AGA TTG 747 Pro Phe Ala His He Pro Leu Gin Asn Phe Glu Asn Asn Pro Arg Leu 190 195 200 GAG GGA CCG GAA TTA CTC GGT CTT GCA AGC TAC GAC ACT AAC TGC ACC 795 Glu Gly Pro Glu Leu Leu Gly Leu Ala Ser Tyr Asp Thr Asn Cys Thr 205 210 215 TGAAACAACT GGCAAAACCT GAAAATGAAG AATTGGGGGG TGACLT1U1Α ACaVACACTTC 855 ACCACTTTAT CAAATATCAC ATCTATTATG TAATAAGTAT ATATATCTAG TAAAAACAAA 915 AAAAATGAAG AATCGAATCG CTAATATCAT CTGGTCTCAA TTGAGAACTT CGAGGTCTCT 975 ATGTAAAATT TCTAAATGCG ATTTTCGCTT ACTCTAATCT TCGGTTGTGG GATTCTGAGA 1035 AGTAACATTT CTATTGCTAT GCTATCAACT TGTTCTGCCT TGTCTGCAAA AAAAAAAAAA 1095 AAAAAAAAAA A 1106 (2) INFORMATTCN FOR SEQ ID NO: 23: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 218 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID ND: 23: Met Ala Ser Arg Asn Tyr Arg Trp Glu Leu Phe Ala Ala Ser Leu Thr 1 5 10 15 Leu Thr Leu Ala Leu He His Leu Val Glu Ala Asn Ser Glu Gly Asp 20 25 30 Ala Leu Tyr Ala Leu Arg Arg Ser Leu Thr Asp Pro Asp His Val Leu 35 40 45 Gin Ser Trp Asp Pro Thr Leu Val Asn Pro Cys Thr Trp Phe His Val 50 55 60 Thr Cys Asn Gin Asp Asn Arg Val Thr Arg Val Asp Leu Gly Asn Ser 65 70 75 80 Asn Leu Ser Gly His Leu Ala Pro Glu Leu Gly Lys Leu Glu His Leu 85 90 95 Gin Tyr Leu Glu Leu Tyr Lys Asn Asn He Gin Gly Thr He Pro Ser 100 105 110 Glu Leu Gly Asn Leu Lys Asn Leu He Ser Leu Asp Leu Tyr Asn Asn 115 120 125 Asn Leu Thr Gly He Val Pro Thr Phe Leu Gly Lys Leu Lys Ser Leu 130 135 140 Val Phe Leu Arg Leu Asn Asp Asn Arg Leu Thr Gly Pro He Leu Glu 145 150 155 160 His Ser Arg Gin Ser Gin Ala Phe Lys Val Val Asp Val Ser Ser Asn 165 170 175 Asp Leu Cys Gly Thr He Pro Thr Asn Gly Pro Phe Ala His He Pro 180 185 190 Leu Gin Asn Phe Glu Asn Asn Pro Arg Leu Glu Gly Pro Glu Leu Leu 195 200 205 Gly Leu Ala Ser Tyr Asp Thr Asn Cys Thr 210 215 (2) INFORMATION FOR SEQ ID NO: 24: (i) SEQUENCE CHARACTERISTICS: (A) IiENGTH: 981 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: cDNA to mRNA (iii) HYPOTHETICAL: NO (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 104..757 (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 24: AGTGTGACTA ATTTAGTTTG CTTTCTCCTC TTTGTTCAGA AAATTTTCCC TTTACTCTCA 60 AATTCCTTTT CGATTTCCCT CTCTTAAACC TCCGAAAGCT CAC ATG GCG TCT CGA 115 Met Ala Ser Arg 1 AAC TAT CGG TGG GAG CTC TTC GCA GCT TCG TTA ACC CTA ACC TTA GCT 163 Asn Tyr Arg Trp Glu Leu Phe Ala Ala Ser Leu Thr Leu Thr Leu Ala 5 10 15 20 TTG ATT CAC CTG GTC GAA GCA AAC TCC GAA GGA GAT GCT CTC TAC GCT 211 Leu He His Leu Val Glu Ala Asn Ser Glu Gly Asp Ala Leu Tyr Ala 25 30 35 CTT CGC CGG AGT TTG ACA GAT CCA GAC CAT CTC CTC CAG AGC TGG GAT 259 Leu Arg Arg Ser Leu Thr Asp Pro Asp His Val Leu Gin Ser Trp Asp 40 45 50 CCA ACT CTT GTT AAT CCT TCT ACC TGG TTC CAT GTC ACC TCT AAC CAA 307 Pro Thr Leu Val Asn Pro Cys Thr Trp Phe His Val Thr Cys Asn Gin 55 60 65 GAC AAC CGC GTC ACT CCT GTG GAT TTG GGA AAT TCA AAC CTC TCT GGA 355 Asp Asn Arg Val Thr Arg Val Asp Leu Gly Asn Ser Asn Leu Ser Gly 70 75 80 CAT CTT GCG CCT GAG CTT GGG AAG CTT GAA CAT TTA CAG TAT CTA GAG 403 His Leu Ala Pro Glu Leu Gly Lys Leu Glu His Leu Gin Tyr Leu Glu 85 90 95 100 CTC TAC AAA AAC AAC ATC CAA GGA ACT ATA CCT TCC GAA CTT GGA AAT 451 Leu Tyr Lys Asn Asn He Gin Gly Thr He Pro Ser Glu Leu Gly Asn 105 110 115 CTG AAG AAT CTC ATC AGC TTG GAT CTG TAC AAC AAC AAT CTT ACA GGG 499 Leu Lys Asn Leu He Ser Leu Asp Leu Tyr Asn Asn Asn Leu Thr Gly 120 125 130 ATA GTT CCC ACT TCT TTG GGA AAA TTG AAG TCT CTG GTC TTT TTA CGG 547 He Val Pro Thr Ser Leu Gly Lys Leu Lys Ser Leu Val Phe Leu Arg 135 140 145 CTT AAT GAC AAC CGA TTG ACC GCT CCA ATC CCT AGA GCA CTC ACG GCA 595 Leu Asn Asp Asn Arg Leu Thr Gly Pro He Pro Arg Ala Leu Thr Ala 150 155 160 ATC CCA AGC CTT AAA GTT GTT GAC GTC TCA AGC AAT GAT TTG TCT GGA 643 He Pro Ser Leu Lys Val Val Asp Val Ser Ser Asn Asp Leu Cys Gly 165 170 175 180 ACA ATC CCA ACA AAC GGA CCC TTT GCT CAC ATT CCT TTA CAG AAC TTT 691 Thr He Pro Thr Asn Gly Pro Phe Ala His He Pro Leu Gin Asn Phe 185 190 195 GAG AAC AAC CCG AGA TTG GAG GGA CCG GAA TTA CTC GGT CTT GCA AGC 739 Glu Asn Asn Pro Arg Leu Glu Gly Pro Glu Leu Leu Gly Leu Ala Ser 200 205 210 TAC GAC ACT AAC TGC ACC TGAAACAACT GGCAAAACCT GAAAATGAAG 787 Tyr Asp Thr Asn Cys Thr 215 AATTGGGGGG TGACCTTCTA AGAACACTTC ACCACTTTAT CAAATATCAC ATCTATTATG 847 TAATAACTAT ATATATCTAG TAAAAACAAA AAAAATGAAG AATCGAATCG GTAATATCAT 907 CTGGTCTCAA TTGAGAACTT (D3AGGTCTGT ATCTAAAATT TCTAAATGCG ATTTTCGCCT 967 AAATTACTCA CACT 981 (2) INFORMATION FOR SEQ ID NO: 25: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 218 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 25: Met Ala Ser Arg Asn Tyr Arg Trp Glu Leu Phe Ala Ala Ser Leu Thr 1 5 10 15 Leu Thr Leu Ala Leu He His Leu Val Glu Ala Asn Ser Glu Gly Asp 20 25 30 Ala Leu Tyr Ala Leu Arg Arg Ser Leu Thr Asp Pro Asp His Val Leu 35 40 45 Gin Ser Trp Asp Pro Thr Leu Val Asn Pro Cys Thr Trp Phe His Val 50 55 60 Thr Cys Asn Gin Asp Asn Arg Val Thr Arg Val Asp Leu Gly Asn Ser 65 70 75 80 Asn Leu Ser Gly His Leu Ala Pro Glu Leu Gly Lys Leu Glu His Leu 85 90 95 Gin Tyr Leu Glu Leu Tyr Lys Asn Asn He Gin Gly Thr He Pro Ser 100 105 110 Glu Leu Gly Asn Leu Lys Asn Leu He Ser Leu Asp Leu Tyr Asn Asn 115 120 125 Asn Leu Thr Gly He Val Pro Thr Ser Leu Gly Lys Leu Lys Ser Leu 130 135 140 Val Phe Leu Arg Leu Asn Asp Asn Arg Leu Thr Gly Pro He Pro Arg 145 150 155 160 Ala Leu Thr Ala He Pro Ser Leu Lys Val Val Asp Val Ser Ser Asn 165 170 175 Asp Leu Cys Gly Thr He Pro Thr Asn Gly Pro Phe Ala His He Pro 180 185 190 Leu Gin Asn Phe Glu Asn Asn Pro Arg Leu Glu Gly Pro Glu Leu Leu 195 200 205 Gly Leu Ala Ser Tyr Asp Thr Asn Cys Thr 210 215 (2) INFORMATION FOR SEQ ID NO: 26: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 789 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: cDNA to mRNA (iii) HYPOTHETICAL: NO (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 2..661 (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 26: T CGA CCC ACG CGT CCG CGA AAC TAT CGG TGG GAG CTC TTC GCA GCT 46 Arg Pro Thr Arg Pro Arg Asn Tyr Arg Trp Glu Leu Phe Ala Ala 1 5 10 15 TCG TTA ATC CTA ACC TTA GCT TTG ATT CAC CTG GTC GAA GCA AAC TCC 94 Ser Leu He Leu Thr Leu Ala Leu He His Leu Val Glu Ala Asn Ser 20 25 30 GAA GGA GAT GCT CTT TAC GCT CTT CGC CGG AGT TTA ACA GAT CCG GAC 142 Glu Gly Asp Ala Leu Tyr Ala Leu Arg Arg Ser Leu Thr Asp Pro Asp 35 40 45 CAT GTT CTC CAG AGC TGG GAT CCA ACT CTT CTT AAT CCT TGT ACC TGG 190 His Val Leu Gin Ser Trp Asp Pro Thr Leu Val Asn Pro Cys Thr Trp 50 55 60 TTC CAT GTC ACC TGT AAC CAA GAC AAC CGC GTC ACT CGT GTG GAT TTG 238 Phe His Val Thr Cys Asn Gin Asp Asn Arg Val Thr Arg Val Asp Leu 65 70 75 GGG AAT TCA AAC CTC TCT GGA CAT CTT GOT CCT GAG CTT C<ΪGAAG CIT 286 Gly Asn Ser Asn Leu Ser Gly His Leu Ala Pro Glu Leu Gly Lys Leu 80 85 90 95 GAA CAT TTA CAG TAT CTA GAG CTC TAC AAA AAC AAC ATC CAA GGA ACT 334 Glu His Leu Gin Tyr Leu Glu Leu Tyr Lys Asn Asn He Gin Gly Thr 100 105 110 ATA CCT TCC GAA CTT GGA AAT CTG AAG AAT CTC ATC AGC TTG GAT CTG 382 He Pro Ser Glu Leu Gly Asn Leu Lys Asn Leu He Ser Leu Asp Leu 115 120 125 TAC AAC AAC AAT CTT ACA GGG ATA GTT CCC ACT TCT TTG GGA AAA TTG 430 Tyr Asn Asn Asn Leu Thr Gly He Val Pro Thr Ser Leu Gly Lys Leu 130 135 140 AAG TCT CTG GTC TTT TTA CGG CTT AAT GAC AAC CGA TTG ACG GGG CCA 478 Lys Ser Leu Val Phe Leu Arg Leu Asn Asp Asn Arg Leu Thr Gly Pro 145 150 155 ATC CCT AGA GCA CTC ACT GCA ATC CCA AGC CTT AAA GTT GTT GAT GTC 526 He Pro Arg Ala Leu Thr Ala He Pro Ser Leu Lys Val Val Asp Val 160 165 170 175 TCA AGC AAT GAT TTG TCT GGA ACA ATC CCA ACA AAC GGA CCT TTT GCT 574 Ser Ser Asn Asp Leu Cys Gly Thr He Pro Thr Asn Gly Pro Phe Ala 180 185 190 CAC ATT CCT TTA CAG AAC TTT GAG AAC AAC CCG AGG TTG GAG GGA CCG 622 His He Pro Leu Gin Asn Phe Glu Asn Asn Pro Arg Leu Glu Gly Pro 195 200 205 GAA TTA CTC GCT CTT GCA AGC TAC GAC ACT AAC TGC ACC TGAAAAAATT 671 Glu Leu Leu Gly Leu Ala Ser Tyr Asp Thr Asn Cys Thr 210 215 220 GGCAAAACCT GAAAATGAAG AATTGGGGGG TGACCTTCTA ACAAC.ACTTC ACCACTTTAT 731 CAAATATCAC ATCTACTATG TAATAAGTAT ATATATCTAG TCCAAAAAAA AAAAAAAA 789 (2) INFORMATION FOR SEQ ID NO: 27: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 220 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 27: Arg Pro Thr Arg Pro Arg Asn Tyr Arg Trp Glu Leu Phe Ala Ala Ser 1 5 10 15 Leu He Leu Thr Leu Ala Leu He His Leu Val Glu Ala Asn Ser Glu 20 25 30 Gly Asp Ala Leu Tyr Ala Leu Arg Arg Ser Leu Thr Asp Pro Asp His 35 40 45 Val Leu Gin Ser Trp Asp Pro Thr Leu Val Asn Pro Cys Thr Trp Phe 50 55 60 His Val Thr Cys Asn Gin Asp Asn Arg Val Thr Arg Val Asp Leu Gly 65 70 75 80 Asn Ser Asn Leu Ser Gly His Leu Ala Pro Glu Leu Gly Lys Leu Glu 85 90 95 His Leu Gin Tyr Leu Glu Leu Tyr Lys Asn Asn He Gin Gly Thr He 100 105 110 Pro Ser Glu Leu Gly Asn Leu Lys Asn Leu He Ser Leu Asp Leu Tyr 115 120 125 Asn Asn Asn Leu Thr Gly He Val Pro Thr Ser Leu Gly Lys Leu Lys 130 135 140 Ser Leu Val Phe Leu Arg Leu Asn Asp Asn Arg Leu Thr Gly Pro He 145 150 155 160 Pro Arg Ala Leu Thr Ala He Pro Ser Leu Lys Val Val Asp Val Ser 165 170 175 Ser Asn Asp Leu Cys Gly Thr He Pro Thr Asn Gly Pro Phe Ala His 180 185 190 He Pro Leu Gin Asn Phe Glu Asn Asn Pro Arg Leu Glu Gly Pro Glu 195 200 205 Leu Leu Gly Leu Ala Ser Tyr Asp Thr Asn Cys Thr 210 215 220 (2) INFORMATTCN FOR SEQ ID NO: 28: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 894 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: cTNA to mRNA (iii) HYPOTHETICAL: NO (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATION: 1..675 (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 28: GGA CCG ATT CAA GCC TCC GAA GGG GAC GCT CTT CAC GCG CTT CGC CGG 48 Gly Pro He Gin Ala Ser Glu Gly Asp Ala Leu His Ala Leu Arg Arg 1 5 10 15 AGC TTA TCA GAT CCA GAC AAT GTT GTT CAG AGT TGG GAT CCA ACT CTT 96 Ser Leu Ser Asp Pro Asp Asn Val Val Gin Ser Trp Asp Pro Thr Leu 20 25 30 GTT AAT CCT TCT ACT TGG TTT CAT GTC ACT TCT AAT CAA CAC CAT CAA 144 Val Asn Pro Cys Thr Trp Phe His Val Thr Cys Asn Gin His His Gin 35 40 45 GTC ACT CGT CTG GAT TTG GGG AAT TCA AAC TTA TCT GGA CAT CTA GTA 192 Val Thr Arg Leu Asp Leu Gly Asn Ser Asn Leu Ser Gly His Leu Val 50 55 60 CCT GAA CTT GGG AAG CTT GAA CAT TTA CAA TAT CTG TAT GGA ATC ATC 240 Pro Glu Leu Gly Lys Leu Glu His Leu Gin Tyr Leu Tyr Gly He He 65 70 75 80 ACT CTT TTG CCT TTT GAT TAT CTG AAA ACA TTT ACA TTA TCA GTC ACA 288 Thr Leu Leu Pro Phe Asp Tyr Leu Lys Thr Phe Thr Leu Ser Val Thr 85 90 95 CAT ATA ACA TTT TGC TTT GAG TCA TAT ACT GAA CTC TAC AAA AAC GAG 336 His He Thr Phe Cys Phe Glu Ser Tyr Ser Glu Leu Tyr Lys Asn Glu 100 105 110 ATT CAA GGA ACT ATA CCT TCT GAG CTT GGA AAT CTG AAG ACT CTA ATC 384 He Gin Gly Thr He Pro Ser Glu Leu Gly Asn Leu Lys Ser Leu He 115 120 125 AGT TTG GAT CTG TAC AAC AAC AAT CTC ACC GGG AAA ATC CCA TCT TCT 432 Ser Leu Asp Leu Tyr Asn Asn Asn Leu Thr Gly Lys He Pro Ser Ser 130 135 140 TTG GGA AAA TTG AAG TCA CTT GTT TTT TTG CGG CTT AAC GAA AAC CGA 480 Leu Gly Lys Leu Lys Ser Leu Val Phe Leu Arg Leu Asn Glu Asn Arg 145 150 155 160 TTG ACC GGT CCT ATT CCT AGA GAA CTC ACA GTT ATT TCA AGC CTT AAA 528 Leu Thr Gly Pro He Pro Arg Glu Leu Thr Val He Ser Ser Leu Lys 165 170 175 GTT GTT GAT GTC TCA GGG AAT GAT TTG TCT GGA ACA ATT CCA GTA GAA 576 Val Val Asp Val Ser Gly Asn Asp Leu Cys Gly Thr He Pro Val Glu 180 185 190 GGA CCT TTT GAA CAC ATT CCT ATG CAA AAC TTT GAG AAC AAC CTG AGA 624 Gly Pro Phe Glu His He Pro Met Gin Asn Phe Glu Asn Asn Leu Arg 195 200 205 TTG GAG GGA CCA GAA CTA CTA GGT CTT GCG AGC TAT GAC ACC AAT TGC 672 Leu Glu Gly Pro Glu Leu Leu Gly Leu Ala Ser Tyr Asp Thr Asn Cys 210 215 220 ACT TAAAAAGAAG TTGAAGAACC TATAAAGAAG AATGTTAGCT GACCTTGTAA 725 Thr 225 GAACTCTCTA CCAAGTGTTT GTAAATCTAT ATAGAGCCTT GTTTCATGTT ATATATGAAA 785 GCTTTGAGAG ACAGTAACTT GCAATGTATT GCTATTGGTA GAAAAACTTG AAATGAGAAT 845 TAA TTGGATTTGT GTTICTTATG TAACTTGAAT TTCTTATTA 894 (2 ) INFORMATION FOR SEQ ID NO : 29 : (i ) SEQUENCE O-ARACTERISTICS : (A) LENGTH: 225 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 29: Gly Pro He Gin Ala Ser Glu Gly Asp Ala Leu His Ala Leu Arg Arg 1 5 10 15 Ser Leu Ser Asp Pro Asp Asn Val Val Gin Ser Trp Asp Pro Thr Leu 20 25 30 Val Asn Pro Cys Thr Trp Phe His Val Thr Cys Asn Gin His His Gin 35 40 45 Val Thr Arg Leu Asp Leu Gly Asn Ser Asn Leu Ser Gly His Leu Val 50 55 60 Pro Glu Leu Gly Lys Leu Glu His Leu Gin Tyr Leu Tyr Gly He He 65 70 75 80 Thr Leu Leu Pro Phe Asp Tyr Leu Lys Thr Phe Thr Leu Ser Val Thr 85 90 95 His He Thr Phe Cys Phe Glu Ser Tyr Ser Glu Leu Tyr Lys Asn Glu 100 105 110 He Gin Gly Thr He Pro Ser Glu Leu Gly Asn Leu Lys Ser Leu He 115 120 125 Ser Leu Asp Leu Tyr Asn Asn Asn Leu Thr Gly Lys He Pro Ser Ser 130 135 140 Leu Gly Lys Leu Lys Ser Leu Val Phe Leu Arg Leu Asn Glu Asn Arg 145 150 155 160 Leu Thr Gly Pro He Pro Arg Glu Leu Thr Val He Ser Ser Leu Lys 165 170 175 Val Val Asp Val Ser Gly Asn Asp Leu Cys Gly Thr He Pro Val Glu 180 185 190 Gly Pro Phe Glu His He Pro Met Gin Asn Phe Glu Asn Asn Leu Arg 195 200 205 Leu Glu Gly Pro Glu Leu Leu Gly Leu Ala Ser Tyr Asp Thr Asn Cys 210 215 220 Thr 225 (2) INFORMATION FOR SEQ ID NO: 30: (i) SEQUENCE CHARACTERISTICS: (A) LEWGTH: 1063 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: single (D) TOPOLOGY: linear (ii) MOLECULE TYPE: cDNA to mRNA (iii) HYPOTHETICAL: NO (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATTON: 106..759 (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 30: TCGACCCACG CGTCCGACGA AACCCTAATT TTGCTTCCTC ATCTTGTTCA GAAAATTACT 60 CAAATTCCTA TTAGATTACT CTCTCTTCGA CCTCCGATAG CTCAC ATG GCG TCT 114 Met Ala Ser CGA AAC TAT CGG TGG GAG CTC TTC GCA GCT TCG TTA ATC CTA ACC TTA 162 Arg Asn Tyr Arg Trp Glu Leu Phe Ala Ala Ser Leu He Leu Thr Leu 5 10 15 GCT TTG ATT CAC CTG GTC GAA GCA AAC TCC GAA GGA GAT GCT CTT TAC 210 Ala Leu He His Leu Val Glu Ala Asn Ser Glu Gly Asp Ala Leu Tyr 20 25 30 35 GCT CTT CGC CGG AGT TTA ACA GAT CCG GAC CAT GTT CTC CAG AGC TGG 258 Ala Leu Arg Arg Ser Leu Thr Asp Pro Asp His Val Leu Gin Ser Trp 40 45 50 GAT CCA ACT CTT GTT AAT CCT TGT ACC TGG TTC CAT GTC ACC TCT AAC 306 Asp Pro Thr Leu Val Asn Pro Cys Thr Trp Phe His Val Thr Cys Asn 55 60 65 CAA GAC AAC CGC GTC ACT CGT GTG GAT TTG GGG AAT TCA AAC CTC TCT 354 Gin Asp Asn Arg Val Thr Arg Val Asp Leu Gly Asn Ser Asn Leu Ser 70 75 80 GGA CAT CTT GCG CCT GAG CTT GGG AAG CTT GAA CAT TTA CAG TAT CTA 402 Gly His Leu Ala Pro Glu Leu Gly Lys Leu Glu His Leu Gin Tyr Leu 85 90 95 GAG CTC TAC AAA AAC AAC ATC CAA GGA ACT ATA CCT TCC GAA CTT GGA 450 Glu Leu Tyr Lys Asn Asn He Gin Gly Thr He Pro Ser Glu Leu Gly 100 105 110 115 AAT CTG AAG AAT CTC ATC AGC TTG GAT CTG TAC AAC AAC AAT CTT ACA 498 Asn Leu Lys Asn Leu He Ser Leu Asp Leu Tyr Asn Asn Asn Leu Thr 120 125 130 GGG ATA GTT CCC ACT TCT TTG GGA AAA TTG AAG TCT CTG GTC TTT TTA 546 Gly He Val Pro Thr Ser Leu Gly Lys Leu Lys Ser Leu Val Phe Leu 135 140 145 CGG CTT AAT GAC AAC CGA TTG ACG GGG CCA ATC CCT AGA GCA CTC ACT 594 Arg Leu Asn Asp Asn Arg Leu Thr Gly Pro He Pro Arg Ala Leu Thr 150 155 160 GCA ATC CCA AGC CTT AAA GTT GTT GAT GTC TCA AGC AAT GAT TTG TGT 642 Ala He Pro Ser Leu Lys Val Val Asp Val Ser Ser Asn Asp Leu Cys 165 170 175 GGA ACA ATC CCA ACA AAC GGA CCT TTT GCT CAC ATT CCT TTA CAG AAC 690 Gly Thr He Pro Thr Asn Gly Pro Phe Ala His He Pro Leu Gin Asn 180 185 190 195 TTT GAG AAC AAC CCG AGG TTG GAG GGA CCG GAA TTA CTC GCT CTT GCA 738 Phe Glu Asn Asn Pro Arg Leu Glu Gly Pro Glu Leu Leu Gly Leu Ala 200 205 210 AGC TAC GAC ACT AAC TGC ACC TGAAAAAATT GGCAAAACCT GAAAATGAAG 789 Ser Tyr Asp Thr Asn Cys Thr 215 AATTGGGGGG TGACCTTCTA AGAACACTTC ACCACTTTAT CAAATATCAC ATCTACTATG 849 TAATAACTAT ATATATCTAG TCCAAAAAAA AAATGAAGAA TCGAATCACT AATATCATCT 909 Q GTCTCAATT GAGAACTTTG AGGTCTGTCT ATCTAAAATT TCTAAATGCG ACTTTCGCGT 969 ACTCTAATCT TCC4GTTGTGG GATTCTGAGA ACTAACATTT CTATTGGTAT GGTATCAAGT 1029 TGTTCTGCCT TGTCTGCAAA AAAAAAAAAA AAAA 1063 (2) INFORMATION FOR SEQ ID NO: 31: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 218 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPTION: SEQ ID ND: 31: Met Ala Ser Arg Asn Tyr Arg Trp Glu Leu Phe Ala Ala Ser Leu He 1 5 10 15 Leu Thr Leu Ala Leu He His Leu Val Glu Ala Asn Ser Glu Gly Asp 20 25 30 Ala Leu Tyr Ala Leu Arg Arg Ser Leu Thr Asp Pro Asp His Val Leu 35 40 45 Gin Ser Trp Asp Pro Thr Leu Val Asn Pro Cys Thr Trp Phe His Val 50 55 60 Thr Cys Asn Gin Asp Asn Arg Val Thr Arg Val Asp Leu Gly Asn Ser 65 70 75 80 Asn Leu Ser Gly His Leu Ala Pro Glu Leu Gly Lys Leu Glu His Leu 85 90 95 Gin Tyr Leu Glu Leu Tyr Lys Asn Asn He Gin Gly Thr He Pro Ser 100 105 110 Glu Leu Gly Asn Leu Lys Asn Leu He Ser Leu Asp Leu Tyr Asn Asn 115 120 125 Asn Leu Thr Gly He Val Pro Thr Ser Leu Gly Lys Leu Lys Ser Leu 130 135 140 Val Phe Leu Arg Leu Asn Asp Asn Arg Leu Thr Gly Pro He Pro Arg 145 150 155 160 Ala Leu Thr Ala He Pro Ser Leu Lys Val Val Asp Val Ser Ser Asn - 90 - 165 170 175 Asp Leu Cys Gly Thr He Pro Thr Asn Gly Pro Phe Ala His He Pro 180 185 190 Leu Gin Asn Phe Glu Asn Asn Pro Arg Leu Glu Gly Pro Glu Leu Leu 195 200 205 Gly Leu Ala Ser Tyr Asp Thr Asn Cys Thr 210 215 (2) INFORMATION FOR SEQ ID NO: 32: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 2089 base pairs (B) TYPE: nucleic acid (C) STRANDEDNESS: double (D) TOPOLOGY: linear (ii) MOLECULE TYPE: cDNA to mRNA (iii) HYPOTHETICAL: NO (iii) ANTI-SENSE: NO (vi) ORIGINAL SOURCE: (A) ORGANISM: Arabidopsis thaliana (vii) IMMEDIATE SOURCE: (B) CLONE: SERK gene cDNA (ix) FEATURE: (A) NAME/KEY: CDS (B) LOCATTON: 195..2069 (xi) SEQUENCE DESCRIPTION: SEQ ID NO: 32: GGATTTTTAT TTΓATTΓTTT ACTCTTTGTT TGTTTTAATG CTAATGGGTT TTTAAAAGGG 60 TTATCGAAAA AATGAGTGAG TTTGTCTTGA GGTTGTCTCT CTAAAGTGTT AATGGTGGTG 120 ATTTTCGGAA GITAGGGTTT TCTCGGATCT GAAGAGATCA AATCAAGATT CGAAATTTAC 180 (CATTGTTGTT TGAA ATG GAG TCG AGT TAT GTG GTG TTT ATC TTA CTT TCA 230 Met Glu Ser Ser Tyr Val Val Phe He Leu Leu Ser 1 5 10 CTG ATC TTA CTT CCG AAT CAT TCA CTG TGG CTT GCT TCT GCT AAT TTG 278 Leu He Leu Leu Pro Asn His Ser Leu Trp Leu Ala Ser Ala Asn Leu 15 20 25 GAA GCT GAT GCT TTG CAT ACT TTG AGG GTT ACT CTA GTT GAT CCA AAC 326 Glu Gly Asp Ala Leu His Thr Leu Arg Val Thr Leu Val Asp Pro Asn 30 35 40 AAT GTC TTG CAG AGC TGG GAT CCT ACG CTA GTG AAT CCT TGC ACA TGG 374 Asn Val Leu Gin Ser Trp Asp Pro Thr Leu Val Asn Pro Cys Thr Trp 45 50 55 60 TTC CAT GTC ACT TGC AAC AAC GAG AAC AGT GTC ATA AGA GTT GAT TTG 422 Phe His Val Thr Cys Asn Asn Glu Asn Ser Val He Arg Val Asp Leu 65 70 75 GGG AAT GCA GAG TTA TCT GGC CAT TTA GTT CCA GAG CTT GGT GTG CTC 470 Gly Asn Ala Glu Leu Ser Gly His Leu Val Pro Glu Leu Gly Val Leu 80 85 90 AAG AAT TTG CAG TAT TTG GAG CTT TAC AGT AAC AAC ATA ACT GGC CCG 518 Lys Asn Leu Gin Tyr Leu Glu Leu Tyr Ser Asn Asn He Thr Gly Pro 95 100 105 ATT CCT ACT AAT CTT GGA AAT CTG ACA AAC TTA GTG AGT TTG GAT CTT 566 - 92 - Ile Pro Ser Asn Leu Gly Asn Leu Thr Asn Leu Val Ser Leu Asp Leu 110 115 120 TAC TTA AAC AGC TTC TCC GGT CCT ATT CCG GAA TCA TTG GGA AAG CTT 614 Tyr Leu Asn Ser Phe Ser Gly Pro He Pro Glu Ser Leu Gly Lys Leu 125 130 135 140 TCA AAG CTG AGA TTT CTC CGG CTT AAC AAC AAC ACT CTC ACT GGG TCA 662 Ser Lys Leu Arg Phe Leu Arg Leu Asn Asn Asn Ser Leu Thr Gly Ser 145 150 155 ATT CCT ATG TCA CTG ACC AAT ATT ACT ACC CTT CAA GTG TTA GAT CTA 710 He Pro Met Ser Leu Thr Asn He Thr Thr Leu Gin Val Leu Asp Leu 160 165 170 TCA AAT AAC AGA CTC TCT GGT TCA GTT CCT GAC AAT GGC TCC TTC TCA 758 Ser Asn Asn Arg Leu Ser Gly Ser Val Pro Asp Asn Gly Ser Phe Ser 175 180 185 CTC TTC ACA CCC ATC AGT TTT GCT AAT AAC TTA GAC CTA TCT GGA CCT 806 Leu Phe Thr Pro He Ser Phe Ala Asn Asn Leu Asp Leu Cys Gly Pro 190 195 200 GTT ACA AGT CAC CCA TCT CCT GGA TCT CCC CCG TTT TCT CCT CCA CCA 854 Val Thr Ser His Pro Cys Pro Gly Ser Pro Pro Phe Ser Pro Pro Pro 205 210 215 220 CCT TTT ATT CAA CCT CCC CCA GTT TCC ACC CCG ACT GGG TAT GGT ATA 902 Pro Phe He Gin Pro Pro Pro Val Ser Thr Pro Ser Gly Tyr Gly He 225 230 235 ACT GGA GCA ATA GCT GGT GGA GTT GCT GCA GGT GCT GCT TTG CCC TTT 950 Thr Gly Ala He Ala Gly Gly Val Ala Ala Gly Ala Ala Leu Pro Phe 240 245 250 GCT GCT CCT GCA ATA GCC TTT GCT TGG TGG CGA CGA AGA AGC CCA CTA 998 Ala Ala Pro Ala He Ala Phe Ala Trp Trp Arg Arg Arg Ser Pro Leu 255 260 265 GAT ATT TTC TTC GAT GTC CCT GCC GAA GAA GAT CCA GAA GTT CAT CTG 1046 Asp He Phe Phe Asp Val Pro Ala Glu Glu Asp Pro Glu Val His Leu 270 275 280 GGA CAG CTC AAG AGG TTT TCT TTG CGG GAG CTA CAA GTG GCG ACT GAT 1094 Gly Gin Leu Lys Arg Phe Ser Leu Arg Glu Leu Gin Val Ala Ser Asp 285 290 295 300 GGG TTT AGT AAC AAG AAC ATT TTG GGC AGA GCT GGG TTT GGG AAA GTC 1142 Gly Phe Ser Asn Lys Asn He Leu Gly Arg Gly Gly Phe Gly Lys Val 305 310 315 TAC AAG GGA CGC TTG GCA GAC GGA ACT CTT GTT GCT GTC AAG AGA CTG 1190 Tyr Lys Gly Arg Leu Ala Asp Gly Thr Leu Val Ala Val Lys Arg Leu 320 325 330 AAG GAA GAG CGA ACT CCA GCT GGA GAG CTC CAG TTT CAA ACA GAA CTA 1238 Lys Glu Glu Arg Thr Pro Gly Gly Glu Leu Gin Phe Gin Thr Glu Val 335 340 345 GAG ATG ATA AGT ATG GCA GTT CAT CGA AAC CTG TTG AGA TTA CGA GGT 1286 Glu Met He Ser Met Ala Val His Arg Asn Leu Leu Arg Leu Arg Gly 350 355 360 TTC TGT ATG ACA CCG ACC GAG AGA TTG CTT GTG TAT CCT TAC ATG GCC 1334 Phe Cys Met Thr Pro Thr Glu Arg Leu Leu Val Tyr Pro Tyr Met Ala 365 370 375 380 AAT GGA AGT GTT GCT TCG TGT CTC AGA GAG AGG CCA CCG TCA CAA CCT 1382 Asn Gly Ser Val Ala Ser Cys Leu Arg Glu Arg Pro Pro Ser Gin Pro 385 390 395 CCG CTT GAT TGG CCA ACG CGG AAG AGA ATC GCG CTA GGC TCA GCT CGA 1430 Pro Leu Asp Trp Pro Thr Arg Lys Arg He Ala Leu Gly Ser Ala Arg 400 405 410 GGT TTG TCT TAC CTA CAT GAT CAC TGC GAT CCG AAG ATC ATT CAC CCT 1478 Gly Leu Ser Tyr Leu His Asp His Cys Asp Pro Lys He He His Arg 415 420 425 GAC GTA AAA GCA GCA AAC ATC CTC TTA GAC GAA GAA TTC GAA GCG GTT 1526 Asp Val Lys Ala Ala Asn He Leu Leu Asp Glu Glu Phe Glu Ala Val 430 435 440 GTT GGA GAT TTC GGG TTG GCA AAG CTT ATG GAC TAT AAA GAC ACT CAC 1574 Val Gly Asp Phe Gly Leu Ala Lys Leu Met Asp Tyr Lys Asp Thr His 445 450 455 460 GTG ACA ACA GCA GTC CCT GGC ACC ATC GGT CAC ATC GCT CCA GAA TAT 1622 Val Thr Thr Ala Val Arg Gly Thr He Gly His He Ala Pro Glu Tyr 465 470 475 CTC TCA ACC GGA AAA TCT TCA GAG AAA ACC GAC GTT TTC GGA TAC GGA 1670 Leu Ser Thr Gly Lys Ser Ser Glu Lys Thr Asp Val Phe Gly Tyr Gly 480 485 490 ATC ATC CTT CTA GAA CTA ATC ACA GGA CAA AGA GCT TTC GAT CTC GCT 1718 He Met Leu Leu Glu Leu He Thr Gly Gin Arg Ala Phe Asp Leu Ala 495 500 505 CGG CTA GCT AAC GAC GAC GAC GTC ATG TTA CTT GAC TGG GTG AAA GGA 1766 Arg Leu Ala Asn Asp Asp Asp Val Met Leu Leu Asp Trp Val Lys Gly 510 515 520 TTG TTG AAG GAG AAG AAG CTA GAG ATG TTA GTG GAT CCA GAT CTT CAA 1814 Leu Leu Lys Glu Lys Lys Leu Glu Met Leu Val Asp Pro Asp Leu Gin 525 530 535 540 ACA AAC TAC GAG GAG AGA GAA CTG GAA CAA GTG ATA CAA CTG GCG TTG 1862 Thr Asn Tyr Glu Glu Arg Glu Leu Glu Gin Val He Gin Val Ala Leu 545 550 555 T/EP97/0 43 - 95 - CTA TGC ACG CAA GGA TCA CCA ATG GAA AGA CCA AAG ATG TCT GAA GTT 1910 Leu Cys Thr Gin Gly Ser Pro Met Glu Arg Pro Lys Met Ser Glu Val 560 565 570 CTA AGG ATG CTG GAA GGA GAT GGG CTT GCG GAG AAA TGG GAC GAA TGG 1958 Val Arg Met Leu Glu Gly Asp Gly Leu Ala Glu Lys Trp Asp Glu Trp 575 580 585 CAA AAA GTT GAG ATT TTG AGG GAA GAG ATT GAT TTG ACT CCT AAT CCT 2006 Gin Lys Val Glu He Leu Arg Glu Glu He Asp Leu Ser Pro Asn Pro 590 595 600 AAC TCT GAT TGG ATT CTT GAT TCT ACT TAC AAT TTG CAC GCC GTT GAG 2054 Asn Ser Asp Trp He Leu Asp Ser Thr Tyr Asn Leu His Ala Val Glu 605 610 615 620 TTA TCT GCT CCA AGG TAAAAAAAAA AAAAAAAAAA 2089 Leu Ser Gly Pro Arg 625 (2) INFORMATION FOR SEQ ID NO: 33: (i) SEQUENCE CHARACTERISTICS: (A) LENGTH: 625 amino acids (B) TYPE: amino acid (D) TOPOLOGY: linear (ii) MOLECULE TYPE: protein (xi) SEQUENCE DESCRIPπON: SEQ ID NO: 33: Met Glu Ser Ser Tyr Val Val Phe He Leu Leu Ser Leu He Leu Leu 1 5 10 15 Pro Asn His Ser Leu Trp Leu Ala Ser Ala Asn Leu Glu Gly Asp Ala 20 25 30 Leu His Thr Leu Arg Val Thr Leu Val Asp Pro Asn Asn Val Leu Gin 35 40 45 Ser Trp Asp Pro Thr Leu Val Asn Pro Cys Thr Trp Phe His Val Thr 50 55 60 Cys Asn Asn Glu Asn Ser Val He Arg Val Asp Leu Gly Asn Ala Glu 65 70 75 80 Leu Ser Gly His Leu Val Pro Glu Leu Gly Val Leu Lys Asn Leu Gin 85 90 95 Tyr Leu Glu Leu Tyr Ser Asn Asn He Thr Gly Pro He Pro Ser Asn 100 105 110 Leu Gly Asn Leu Thr Asn Leu Val Ser Leu Asp Leu Tyr Leu Asn Ser 115 120 125 Phe Ser Gly Pro He Pro Glu Ser Leu Gly Lys Leu Ser Lys Leu Arg 130 135 140 Phe Leu Arg Leu Asn Asn Asn Ser Leu Thr Gly Ser He Pro Met Ser 145 150 155 160 Leu Thr Asn He Thr Thr Leu Gin Val Leu Asp Leu Ser Asn Asn Arg 165 170 175 Leu Ser Gly Ser Val Pro Asp Asn Gly Ser Phe Ser Leu Phe Thr Pro 180 185 190 He Ser Phe Ala Asn Asn Leu Asp Leu Cys Gly Pro Val Thr Ser His 195 200 205 Pro Cys Pro Gly Ser Pro Pro Phe Ser Pro Pro Pro Pro Phe He Gin 210 215 220 Pro Pro Pro Val Ser Thr Pro Ser Gly Tyr Gly He Thr Gly Ala He 225 230 235 240 Ala Gly Gly Val Ala Ala Gly Ala Ala Leu Pro Phe Ala Ala Pro Ala 245 250 255 He Ala Phe Ala Trp Trp Arg Arg Arg Ser Pro Leu Asp He Phe Phe 260 265 270 Asp Val Pro Ala Glu Glu Asp Pro Glu Val His Leu Gly Gin Leu Lys 275 280 285 Arg Phe Ser Leu Arg Glu Leu Gin Val Ala Ser Asp Gly Phe Ser Asn 290 295 300 Lys Asn He Leu Gly Arg Gly Gly Phe Gly Lys Val Tyr Lys Gly Arg 305 310 315 320 Leu Ala Asp Gly Thr Leu Val Ala Val Lys Arg Leu Lys Glu Glu Arg 325 330 335 Thr Pro Gly Gly Glu Leu Gin Phe Gin Thr Glu Val Glu Met He Ser 340 345 350 Met Ala Val His Arg Asn Leu Leu Arg Leu Arg Gly Phe Cys Met Thr 355 360 365 Pro Thr Glu Arg Leu Leu Val Tyr Pro Tyr Met Ala Asn Gly Ser Val 370 375 380 Ala Ser Cys Leu Arg Glu Arg Pro Pro Ser Gin Pro Pro Leu Asp Trp 385 390 395 400 Pro Thr Arg Lys Arg He Ala Leu Gly Ser Ala Arg Gly Leu Ser Tyr 405 410 415 Leu His Asp His Cys Asp Pro Lys He He His Arg Asp Val Lys Ala - 98 - 420 425 430 Ala Asn He Leu Leu Asp Glu Glu Phe Glu Ala Val Val Gly Asp Phe 435 440 445 Gly Leu Ala Lys Leu Met Asp Tyr Lys Asp Thr His Val Thr Thr Ala 450 455 460 Val Arg Gly Thr He Gly His He Ala Pro Glu Tyr Leu Ser Thr Gly 465 470 475 480 Lys Ser Ser Glu Lys Thr Asp Val Phe Gly Tyr Gly He Met Leu Leu 485 490 495 Glu Leu He Thr Gly Gin Arg Ala Phe Asp Leu Ala Arg Leu Ala Asn 500 505 510 Asp Asp Asp Val Met Leu Leu Asp Trp Val Lys Gly Leu Leu Lys Glu 515 520 525 Lys Lys Leu Glu Met Leu Val Asp Pro Asp Leu Gin Thr Asn Tyr Glu 530 535 540 Glu Arg Glu Leu Glu Gin Val He Gin Val Ala Leu Leu Cys Thr Gin 545 550 555 560 Gly Ser Pro Met Glu Arg Pro Lys Met Ser Glu Val Val Arg Met Leu 565 570 575 Glu Gly Asp Gly Leu Ala Glu Lys Trp Asp Glu Trp Gin Lys Val Glu 580 585 590 He Leu Arg Glu Glu He Asp Leu Ser Pro Asn Pro Asn Ser Asp Trp 595 600 605 He Leu Asp Ser Thr Tyr Asn Leu His Ala Val Glu Leu Ser Gly Pro 610 615 620 Arg 625 - 100 - REFERENCES Aleith, F. and Richter, G. 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Claims: What is Claimed is: 1. A method of producing apomictic seeds comprising the steps of: (i) transforming plant material with a nucleotide sequence encoding a protein the presence of which in an active form in a cell, or membrane thereof, renders said cell embryogenic, (ii) regenerating the thus transformed material into plants, or carpel-containing parts thereof, and (iii) expressing the sequence in the vicinity of the embryo sac. 2. A method according to the preceding claim, wherein the apomictic seeds are of the adventitious embryony type. 3. A method according to either of the preceding claims, wherein expression of the sequence yields a protein kinase capable of spanning a plant cell membrane. 4. A method according to the preceding claim wherein the kinase is capable of autophosphorylation. 5. A method according to any of the preceding claims, wherein the protein is a leucine rich repeat receptor like kinase and comprises a ligand binding domain, a proline box, a transmembrane domain, a kinase domain and a protein binding domain. 6. A method according to the preceding claim, wherein the protein lacks a functional ligand binding domain but comprises a proline box, a transmembrane domain, a kinase domain and a protein binding domain. 7. A method according to any preceding claim, wherein once incoφorated into the cell membrane, the protein binding domain is located intra-cellularly. 8. A method according to any preceding claim, wherein the sequence further encodes a cell membrane targeting sequence. - 104 - 9. A method according to any preceding claim, wherein the sequence is that depicted in SEQ ID Nos. 1 or 2 or is complementary to one which hybridizes under stringent conditions with the said sequences and which encodes a membrane bound protein having kinase activity. 10. A method according to any preceding claim, wherein the sequence is modified in that known mRNA instability motifs or polyadenylation signals are removed and/or codons which are preferred by the plant into which the sequence is to be inserted are used so that expression of the thus modified sequence in the said plant yields substantially similar protein to that obtained by expression of the unmodified sequence in the organism in which the protein is endogenous. 11. A method according to any preceding claim, wherein expression of the sequence is under control of an inducible or developmentally regulated promoter. 12. A method according to the preceding claim, wherein expression of the sequence is under control of one of the following: a promoter which regulates expression of SERK genes in planta, the carrot chitinase DcEP3-1 gene promoter, the Arabidopsis AtChitlV gene promoter, the Arabidopsis LTP-1 gene promoter, the Arabidopsis bel-1 gene promoter, the petunia fbp-7 gene promoter, the Arabidopsis ANT gene promoter, the promoter of the 0126 gene from Phalaenopsis. 13. A method according to any of the preceding claims, wherein the sequence is expressed in the somatic cells of the embryo sac, ovary wall, nucellus, or integuments. 14. A method according to any of the preceding claims, wherein the endosperm within the apomictic seed results from fusion of polar nuclei within the embryo sac with a pollen- derived male gamete nucleus. 15. A method according to the preceding claim, wherein the sequence encoding the protein is expressed prior to fusion of the polar nuclei with the male gamete nucleus. 16. DNA comprising a sequence encoding a protein the presence of which in an active form in a cell, or membrane thereof, renders said cell embryogenic. 17. DNA according to claim 16, wherein the protein is a leucine rich repeat receptor like kinase and comprises a ligand binding domain, a proline box, a transmembrane domain, a kinase domain and a protein binding domain, the ligand binding domain optionally being absent or functionally inactive. 18. DNA according to either of daims 16 or 17 comprising a DNA sequence encoding a N- terminal protein fragment having the following amino acid sequence: Gh Ser Trp Asp Pro Thr Leu Val Asn Pro Cys ThrTrp Phe HB Val Thr Cys Asa 19. DNA according to claim 18 comprising a DNA sequence encoding a N-terminal protein fragment having the following amino add sequence: Val Xaa Gh Ser Trp Asp Pro Thr Leu Val Asn Pro Cys ThrTrp Phe Hrs Val Thr Cys Asn with Xaa being a variable amino acid, but preferably Leu or Val 20. DNA according to claim 19 comprising a DNA sequence encoding a N-terminal protein fragment having the following amino acid sequence: Val Xaa Gh Ser Trp Asp Pro Thr Leu Val Asn Pro Cys Thr Trp Phe His Val Thr Cys Asn Xab Xac Xad Xae Val Xaf Arg Val Asp Leu Gly Asn Xag Xah Leu Ser Gly HE Leu Xai Pro Glu Leu Gly Xaj Leu Xak Xal Leu Gh with Xaa to Xak being a variable amino acid, but preferably Xaa = Leu or Val Xab=AsnorGh Xac = GkjorAsporHis Xad= Asn or He Xae = Ser or Arg or Gh Xaf = leorThr Xag = Ala or Ser Xai = Val or Ala Xaj=ValorLys Xak=LysorGlu Xal=AsnorHis 21. DNA comprising a sequence encoding a protein having the sequence depicted in SEQ ID No. 3, or a protein substantially similar thereto which is capable of being membrane bound and which has kinase activity. 22. DNA comprising a sequence encoding a protein having the sequence depicted in SEQ ID No. 21 , or a protein substantially similar thereto which is capable of being membrane bound and which has kinase activity. 23. DNA comprising a sequence encoding a protein having the sequence depicted in SEQ ID No. 33, or a protein substantially similar thereto which is capable of being membrane bound and which has kinase activity. 24. DNA comprising a sequence encoding a protein having the sequence depicted in SEQ ID Nos. 23, 25, 27, 29 and 31 , or a protein substantially similar thereto which is capable of being membrane bound and which has kinase adivity. 25. DNA according to any preceding claim, comprising a DNA having the sequence depicted in SEQ ID Nos. 1 or 2 or a sequence which is complementary to one which hybridizes under stringent conditions with the said sequences and which encodes a membrane bound protein having kinase activity. 26. DNA according to any preceding claim, comprising a DNA having the sequence depicted in SEQ ID No: 20 or a sequence which is complementary to one which hybridizes under stringent conditions with the said sequences and which encodes a membrane bound protein having kinase activity. 27. DNA according to any preceding daim, comprising a DNA having the sequence depicted in SEQ ID No: 32 or a sequence which is complementary to one which hybridizes under stringent conditions with the said sequences and which encodes a membrane bound protein having kinase activity. 28. DNA according to any preceding claim, comprising a DNA having the sequence depided in SEQ ID Nos: 22, 24, 26, 28 and 30 or a sequence which is complementary to one which hybridizes under stringent conditions with the said sequences and which encodes a membrane bound protein having kinase activity. 29. DNA according to any of the preceding claims, which further encodes a cell membrane targeting sequence. 30. DNA according to any one of the preceding claims, in which the protein encoding region is under expression control of a developmentally regulated or inducible promoter. 31. DNA according to claim 30, wherein the promoter is one of the following: a promoter which regulates expression of SERK genes in planta, the carrot chitinase DcEP3-1 gene promoter, the Arabidopsis AtChitlV gene promoter, the Arabidopsis LTP-1 gene promoter, the Arabidopsis bel-1 gene promoter, the petunia fbp-7 gene promoter, the Arabidopsis ANT gene promoter, the promoter of the 0126 gene from Phalaenopsis; the Arabidopsis DMC1 promoter, the pTA7001 inducible promoter. 32. DNA according to any preceding claim, wherein said DNA is a recombinant DNA. 33. DNA according to any preceding claim, wherein the sequence is modified in that known mRNA instability motifs or polyadenylation signals are removed and/or codons which are preferred by the plant into which the DNA is to be inserted are used so that expression of the thus modified DNA in the said plant yields substantially similar protein to that obtained by expression of the unmodified DNA in the organism in which the protein is endogenous. 34. DNA which is complementary to that which hybridizes under stringent conditions with the DNA of any one of claims 16 to 29. 35. A vedor containing a DNA sequence as claimed in any one of claims 16 to 34. 36. Plant cell transformed with the DNA of any one of claims 16 to 34 or the vedor of daim 35, which contains the DNA stably incorporated into its genome. 37. Plant cell according to claim 36, which is part of a whole plant. 38. Plants transformed with the DNA of any one of claims 16 to 34 or the vedor of claim 35, the progeny of such plants which contain the DNA stably incoφorated, and/or the apomidic seeds of such plants or such progeny. 39. Plants transformed with the DNA comprised by the recombinant DNA of claims 16 to 34. 40. Use of the DNA of any one of claims 16-34 in the manufacture of apomidic seeds. 41. Plants which are derived from apomidic seeds obtainable by the method of any one of claims 1-15 or 40. 42. A method of obtaining cultivars compπsing the steps of fertilizing plants with the pollen of the plants of either of claims 38, 39 or 40 and cultivars which result from the said method. 43. A method of obtaining embryogenic cells in plant material, compnsing transforming the mateπal with a recombinant DNA sequence as claimed in any one of claims 16-34, the DNA compnsed by the recombinant DNA of any one of claims 16 to 34, or the vedor of claim 35, expressing the sequence in the mateπal or derivatives thereof and subjecting the said material or derivatives to a compound which acts as a ligand for the gene produd of the said sequence. 44. A method according to the preceding claim, wherein the sequence encodes a leucine rich repeat receptor like kinase, and the compound is a phyto-hormone. 45. A method of generating somatic embryos under in vitm conditions wherein the SERK protein is overexpressed ectopically. 46. A bag containing apomidic seeds obtainable by the method of any one of claims 1 -15 or 40.

Inventors: DE VRIES SAPE CORNELIS, HECHT VALERIE FRANCE GABRIELLE, SCHMIDT EDUARD DANIEL LEENDERT, VAN HOLST GERRIT JAN, DE VRIES, SAPE, CORNELIS, HECHT, VALERIE, FRANCE, GABRIELLE, SCHMIDT, EDUARD, DANIEL, LEENDERT, VAN HOLST, GERRIT, JAN
Applicants: CIBA GEIGY AG, HECHT VALERIE FRANCE GABRIELLE, HOLST GERRIT JAN VAN, SCHMIDT EDUARD DANIEL LEENDERT, VRIES SAPE CORNELIS DE, DE VRIES, SAPE, CORNELIS, HECHT, VALERIE, FRANCE, GABRIELLE, NOVARTIS AG, SCHMIDT, EDUARD, DANIEL, LEENDERT, VAN HOLST, GERRIT, JAN
Application year: 1997
Main classification: C12N15
IPC codes: A01H5, C07K14, C12N5, C12N9, C12N15