Skip to main content
PMC home page
Plant Physiology logoLink to Plant Physiology
. 1995 Aug;108(4):1735–1739. doi: 10.1104/pp.108.4.1735

The Pto bacterial resistance gene and the Fen insecticide sensitivity gene encode functional protein kinases with serine/threonine specificity.

Y T Loh 1, G B Martin 1
PMCID: PMC157555  PMID: 7659757

Abstract

The catalytic activity and amino acid specificity of the tomato Pto and Fen kinases were investigated. The Pto and Fen genes were fused to the carboxyl terminus of the maltose-binding protein and expressed in Escherichia coli. Incubation of the purified fusion proteins with [gamma-32P]ATP in an in vitro assay showed that both proteins were capable of autophosphorylation. Mutant fusion proteins in which the conserved lysine residue of subdomain II was changed to a glutamine were unable to autophosphorylate. Phosphoamino analysis of the active fusion proteins indicated that both kinases phosphorylate serine and threonine residues but not tyrosine.

Full Text

The Full Text of this article is available as a PDF (1.7 MB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Ali N., Halfter U., Chua N. H. Cloning and biochemical characterization of a plant protein kinase that phosphorylates serine, threonine, and tyrosine. J Biol Chem. 1994 Dec 16;269(50):31626–31629. [PubMed] [Google Scholar]
  2. Boyle W. J., van der Geer P., Hunter T. Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates. Methods Enzymol. 1991;201:110–149. doi: 10.1016/0076-6879(91)01013-r. [DOI] [PubMed] [Google Scholar]
  3. Chang C., Kwok S. F., Bleecker A. B., Meyerowitz E. M. Arabidopsis ethylene-response gene ETR1: similarity of product to two-component regulators. Science. 1993 Oct 22;262(5133):539–544. doi: 10.1126/science.8211181. [DOI] [PubMed] [Google Scholar]
  4. Chang C., Schaller G. E., Patterson S. E., Kwok S. F., Meyerowitz E. M., Bleecker A. B. The TMK1 gene from Arabidopsis codes for a protein with structural and biochemical characteristics of a receptor protein kinase. Plant Cell. 1992 Oct;4(10):1263–1271. doi: 10.1105/tpc.4.10.1263. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Dwyer K. G., Kandasamy M. K., Mahosky D. I., Acciai J., Kudish B. I., Miller J. E., Nasrallah M. E., Nasrallah J. B. A superfamily of S locus-related sequences in Arabidopsis: diverse structures and expression patterns. Plant Cell. 1994 Dec;6(12):1829–1843. doi: 10.1105/tpc.6.12.1829. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Goring D. R., Rothstein S. J. The S-locus receptor kinase gene in a self-incompatible Brassica napus line encodes a functional serine/threonine kinase. Plant Cell. 1992 Oct;4(10):1273–1281. doi: 10.1105/tpc.4.10.1273. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. 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]
  8. Hanks S. K., Quinn A. M. Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members. Methods Enzymol. 1991;200:38–62. doi: 10.1016/0076-6879(91)00126-h. [DOI] [PubMed] [Google Scholar]
  9. Hirayama T., Oka A. Novel protein kinase of Arabidopsis thaliana (APK1) that phosphorylates tyrosine, serine and threonine. Plant Mol Biol. 1992 Nov;20(4):653–662. doi: 10.1007/BF00046450. [DOI] [PubMed] [Google Scholar]
  10. Horn M. A., Walker J. C. Biochemical properties of the autophosphorylation of RLK5, a receptor-like protein kinase from Arabidopsis thaliana. Biochim Biophys Acta. 1994 Sep 21;1208(1):65–74. doi: 10.1016/0167-4838(94)90160-0. [DOI] [PubMed] [Google Scholar]
  11. Ito Y., Banno H., Moribe T., Hinata K., Machida Y. NPK15, a tobacco protein-serine/threonine kinase with a single hydrophobic region near the amino-terminus. Mol Gen Genet. 1994 Oct 17;245(1):1–10. doi: 10.1007/BF00279745. [DOI] [PubMed] [Google Scholar]
  12. Jung R., Scott M. P., Oliveira L. O., Nielsen N. C. A simple and efficient method for the oligodeoxyribonucleotide-directed mutagenesis of double-stranded plasmid DNA. Gene. 1992 Nov 2;121(1):17–24. doi: 10.1016/0378-1119(92)90157-k. [DOI] [PubMed] [Google Scholar]
  13. Kieber J. J., Rothenberg M., Roman G., Feldmann K. A., Ecker J. R. CTR1, a negative regulator of the ethylene response pathway in Arabidopsis, encodes a member of the raf family of protein kinases. Cell. 1993 Feb 12;72(3):427–441. doi: 10.1016/0092-8674(93)90119-b. [DOI] [PubMed] [Google Scholar]
  14. Lawton M. A., Yamamoto R. T., Hanks S. K., Lamb C. J. Molecular cloning of plant transcripts encoding protein kinase homologs. Proc Natl Acad Sci U S A. 1989 May;86(9):3140–3144. doi: 10.1073/pnas.86.9.3140. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Lin X., Watson J. C. cDNA Sequence of PsPK5, a Protein Kinase Homolog from Pisum sativum L. Plant Physiol. 1992 Oct;100(2):1072–1074. doi: 10.1104/pp.100.2.1072. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Maina C. V., Riggs P. D., Grandea A. G., 3rd, Slatko B. E., Moran L. S., Tagliamonte J. A., McReynolds L. A., Guan C. D. An Escherichia coli vector to express and purify foreign proteins by fusion to and separation from maltose-binding protein. Gene. 1988 Dec 30;74(2):365–373. doi: 10.1016/0378-1119(88)90170-9. [DOI] [PubMed] [Google Scholar]
  17. Martin G. B., Brommonschenkel S. H., Chunwongse J., Frary A., Ganal M. W., Spivey R., Wu T., Earle E. D., Tanksley S. D. Map-based cloning of a protein kinase gene conferring disease resistance in tomato. Science. 1993 Nov 26;262(5138):1432–1436. doi: 10.1126/science.7902614. [DOI] [PubMed] [Google Scholar]
  18. Martin G. B., Frary A., Wu T., Brommonschenkel S., Chunwongse J., Earle E. D., Tanksley S. D. A member of the tomato Pto gene family confers sensitivity to fenthion resulting in rapid cell death. Plant Cell. 1994 Nov;6(11):1543–1552. doi: 10.1105/tpc.6.11.1543. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Mu J. H., Lee H. S., Kao T. H. Characterization of a pollen-expressed receptor-like kinase gene of Petunia inflata and the activity of its encoded kinase. Plant Cell. 1994 May;6(5):709–721. doi: 10.1105/tpc.6.5.709. [DOI] [PMC free article] [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. Stein J. C., Nasrallah J. B. A plant receptor-like gene, the S-locus receptor kinase of Brassica oleracea L., encodes a functional serine/threonine kinase. Plant Physiol. 1993 Mar;101(3):1103–1106. doi: 10.1104/pp.101.3.1103. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Tan J. L., Spudich J. A. Developmentally regulated protein-tyrosine kinase genes in Dictyostelium discoideum. Mol Cell Biol. 1990 Jul;10(7):3578–3583. doi: 10.1128/mcb.10.7.3578. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. 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]
  24. Walker J. C. Receptor-like protein kinase genes of Arabidopsis thaliana. Plant J. 1993 Mar;3(3):451–456. doi: 10.1111/j.1365-313x.1993.tb00164.x. [DOI] [PubMed] [Google Scholar]
  25. 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]
  26. Zhao Y., Feng X. H., Watson J. C., Bottino P. J., Kung S. D. Molecular cloning and biochemical characterization of a receptor-like serine/threonine kinase from rice. Plant Mol Biol. 1994 Nov;26(3):791–803. doi: 10.1007/BF00028849. [DOI] [PubMed] [Google Scholar]

Articles from Plant Physiology are provided here courtesy of Oxford University Press

RESOURCES