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The Plant Cell logoLink to The Plant Cell
. 1992 Oct;4(10):1273–1281. doi: 10.1105/tpc.4.10.1273

The S-locus receptor kinase gene in a self-incompatible Brassica napus line encodes a functional serine/threonine kinase.

D R Goring 1, S J Rothstein 1
PMCID: PMC160214  PMID: 1332796

Abstract

An S-receptor kinase (SRK) cDNA, SRK-910, from the active S-locus in a self-incompatible Brassica napus W1 line has been isolated and characterized. The SRK-910 gene is predominantly expressed in pistils and segregates with the W1 self-incompatibility phenotype in an F2 population derived from a cross between the self-incompatible W1 line and a self-compatible Westar line. Analysis of the predicted amino acid sequence demonstrated that the extracellular receptor domain is highly homologous to S-locus glycoproteins, whereas the cytoplasmic kinase domain contains conserved amino acids present in serine/threonine kinases. An SRK-910 kinase protein fusion was produced in Escherichia coli and found to contain kinase activity. Phosphoamino acid analysis confirmed that only serine and threonine residues were phosphorylated. Thus, the SRK-910 gene encodes a functional serine/threonine receptor kinase.

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Selected References

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  1. Cantley L. C., Auger K. R., Carpenter C., Duckworth B., Graziani A., Kapeller R., Soltoff S. Oncogenes and signal transduction. Cell. 1991 Jan 25;64(2):281–302. doi: 10.1016/0092-8674(91)90639-g. [DOI] [PubMed] [Google Scholar]
  2. Cooper J. A., Sefton B. M., Hunter T. Detection and quantification of phosphotyrosine in proteins. Methods Enzymol. 1983;99:387–402. doi: 10.1016/0076-6879(83)99075-4. [DOI] [PubMed] [Google Scholar]
  3. Douville E. M., Afar D. E., Howell B. W., Letwin K., Tannock L., Ben-David Y., Pawson T., Bell J. C. Multiple cDNAs encoding the esk kinase predict transmembrane and intracellular enzyme isoforms. Mol Cell Biol. 1992 Jun;12(6):2681–2689. doi: 10.1128/mcb.12.6.2681. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Dwyer K. G., Balent M. A., Nasrallah J. B., Nasrallah M. E. DNA sequences of self-incompatibility genes from Brassica campestris and B. oleracea: polymorphism predating speciation. Plant Mol Biol. 1991 Mar;16(3):481–486. doi: 10.1007/BF00024000. [DOI] [PubMed] [Google Scholar]
  5. Hanks S. K., Quinn A. M., Hunter T. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science. 1988 Jul 1;241(4861):42–52. doi: 10.1126/science.3291115. [DOI] [PubMed] [Google Scholar]
  6. Harvey R. J., Darlison M. G. Random-primed cDNA synthesis facilitates the isolation of multiple 5'-cDNA ends by RACE. Nucleic Acids Res. 1991 Jul 25;19(14):4002–4002. doi: 10.1093/nar/19.14.4002. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Johnson D. E., Lee P. L., Lu J., Williams L. T. Diverse forms of a receptor for acidic and basic fibroblast growth factors. Mol Cell Biol. 1990 Sep;10(9):4728–4736. doi: 10.1128/mcb.10.9.4728. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Jones J. D., Dunsmuir P., Bedbrook J. High level expression of introduced chimaeric genes in regenerated transformed plants. EMBO J. 1985 Oct;4(10):2411–2418. doi: 10.1002/j.1460-2075.1985.tb03949.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Kandasamy M. K., Paolillo D. J., Faraday C. D., Nasrallah J. B., Nasrallah M. E. The S-locus specific glycoproteins of Brassica accumulate in the cell wall of developing stigma papillae. Dev Biol. 1989 Aug;134(2):462–472. doi: 10.1016/0012-1606(89)90119-x. [DOI] [PubMed] [Google Scholar]
  10. Karin M. Signal transduction from cell surface to nucleus in development and disease. FASEB J. 1992 May;6(8):2581–2590. doi: 10.1096/fasebj.6.8.1317309. [DOI] [PubMed] [Google Scholar]
  11. Kyte J., Doolittle R. F. A simple method for displaying the hydropathic character of a protein. J Mol Biol. 1982 May 5;157(1):105–132. doi: 10.1016/0022-2836(82)90515-0. [DOI] [PubMed] [Google Scholar]
  12. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  13. Lin H. Y., Wang X. F., Ng-Eaton E., Weinberg R. A., Lodish H. F. Expression cloning of the TGF-beta type II receptor, a functional transmembrane serine/threonine kinase. Cell. 1992 Feb 21;68(4):775–785. doi: 10.1016/0092-8674(92)90152-3. [DOI] [PubMed] [Google Scholar]
  14. Maga E. A., Richardson T. Amplification of a 9.0-kb fragment using PCR. Biotechniques. 1991 Aug;11(2):185–186. [PubMed] [Google Scholar]
  15. Ochman H., Gerber A. S., Hartl D. L. Genetic applications of an inverse polymerase chain reaction. Genetics. 1988 Nov;120(3):621–623. doi: 10.1093/genetics/120.3.621. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Petch L. A., Harris J., Raymond V. W., Blasband A., Lee D. C., Earp H. S. A truncated, secreted form of the epidermal growth factor receptor is encoded by an alternatively spliced transcript in normal rat tissue. Mol Cell Biol. 1990 Jun;10(6):2973–2982. doi: 10.1128/mcb.10.6.2973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Scutt C. P., Croy R. R. An S5 self-incompatibility allele-specific cDNA sequence from Brassica oleracea shows high homology to the SLR2 gene. Mol Gen Genet. 1992 Mar;232(2):240–246. doi: 10.1007/BF00280002. [DOI] [PubMed] [Google Scholar]
  18. Seger R., Ahn N. G., Boulton T. G., Yancopoulos G. D., Panayotatos N., Radziejewska E., Ericsson L., Bratlien R. L., Cobb M. H., Krebs E. G. Microtubule-associated protein 2 kinases, ERK1 and ERK2, undergo autophosphorylation on both tyrosine and threonine residues: implications for their mechanism of activation. Proc Natl Acad Sci U S A. 1991 Jul 15;88(14):6142–6146. doi: 10.1073/pnas.88.14.6142. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Smith D. B., Johnson K. S. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene. 1988 Jul 15;67(1):31–40. doi: 10.1016/0378-1119(88)90005-4. [DOI] [PubMed] [Google Scholar]
  20. Stein J. C., Howlett B., Boyes D. C., Nasrallah M. E., Nasrallah J. B. Molecular cloning of a putative receptor protein kinase gene encoded at the self-incompatibility locus of Brassica oleracea. Proc Natl Acad Sci U S A. 1991 Oct 1;88(19):8816–8820. doi: 10.1073/pnas.88.19.8816. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Tobias C. M., Howlett B., Nasrallah J. B. An Arabidopsis thaliana Gene with Sequence Similarity to the S-Locus Receptor Kinase of Brassica oleracea: Sequence and Expression. Plant Physiol. 1992 May;99(1):284–290. doi: 10.1104/pp.99.1.284. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Ullrich A., Schlessinger J. Signal transduction by receptors with tyrosine kinase activity. Cell. 1990 Apr 20;61(2):203–212. doi: 10.1016/0092-8674(90)90801-k. [DOI] [PubMed] [Google Scholar]
  23. Walker J. C., Zhang R. Relationship of a putative receptor protein kinase from maize to the S-locus glycoproteins of Brassica. Nature. 1990 Jun 21;345(6277):743–746. doi: 10.1038/345743a0. [DOI] [PubMed] [Google Scholar]
  24. Zuberi M. I., Dickinson H. G. Pollen-stigma interaction in Brassica. III. Hydration of the pollen grains. J Cell Sci. 1985 Jun;76:321–336. doi: 10.1242/jcs.76.1.321. [DOI] [PubMed] [Google Scholar]

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