Skip to main content
The Plant Cell logoLink to The Plant Cell
. 1994 May;6(5):709–721. doi: 10.1105/tpc.6.5.709

Characterization of a pollen-expressed receptor-like kinase gene of Petunia inflata and the activity of its encoded kinase.

J H Mu 1, H S Lee 1, T H Kao 1
PMCID: PMC160470  PMID: 8038606

Abstract

From a pollen tube cDNA library of Petunia inflata, we isolated clones encoding a protein with structural features and biochemical properties characteristic of receptor-like kinases. It was designated PRK1 for pollen receptor-like kinase 1. The cytoplasmic domain of PRK1 is highly similar to the kinase domains of other plant receptor-like kinases and contains nearly all of the conserved amino acids for serine/threonine kinases. The extracellular domain of PRK1 contains leucine-rich repeats as found in some other plant receptor-like kinases, but overall its sequence in this region does not share significant similarity. Characterization of a gene encoding PRK1 revealed the presence of two introns. During pollen development, PRK1 mRNA was first detected in anthers containing mostly binucleate microspores; it reached the highest level of mature pollen and remained at a high level in in vitro-germinated pollen tubes. The recombinant cytoplasmic domain of PRK1 autophosphorylated on serine and tyrosine, suggesting that PRK1 may be a dual-specificity kinase. Monospecific immune serum to the recombinant extracellular domain of PRK1 detected a 69-kD protein in microsomal membranes of pollen and pollen tubes. The characteristics of PRK1 suggest that it may play a role in signal transduction events during pollen development and/or pollination.

Full Text

The Full Text of this article is available as a PDF (3.2 MB).

Selected References

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

  1. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1006/abio.1976.9999. [DOI] [PubMed] [Google Scholar]
  2. 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]
  3. Coleman C. E., Kao T. The flanking regions of two Petunia inflata S alleles are heterogeneous and contain repetitive sequences. Plant Mol Biol. 1992 Feb;18(4):725–737. doi: 10.1007/BF00020014. [DOI] [PubMed] [Google Scholar]
  4. 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]
  5. Duerr B., Gawienowski M., Ropp T., Jacobs T. MsERK1: a mitogen-activated protein kinase from a flowering plant. Plant Cell. 1993 Jan;5(1):87–96. doi: 10.1105/tpc.5.1.87. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Featherstone C., Russell P. Fission yeast p107wee1 mitotic inhibitor is a tyrosine/serine kinase. Nature. 1991 Feb 28;349(6312):808–811. doi: 10.1038/349808a0. [DOI] [PubMed] [Google Scholar]
  7. 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]
  8. 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]
  9. Harris P. J., Weinhandl J. A., Clarke A. E. Effect on in Vitro Pollen Growth of an Isolated Style Glycoprotein Associated with Self-Incompatibility in Nicotiana alata. Plant Physiol. 1989 Jan;89(1):360–367. doi: 10.1104/pp.89.1.360. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Hashimoto C., Hudson K. L., Anderson K. V. The Toll gene of Drosophila, required for dorsal-ventral embryonic polarity, appears to encode a transmembrane protein. Cell. 1988 Jan 29;52(2):269–279. doi: 10.1016/0092-8674(88)90516-8. [DOI] [PubMed] [Google Scholar]
  11. 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]
  12. Howell B. W., Afar D. E., Lew J., Douville E. M., Icely P. L., Gray D. A., Bell J. C. STY, a tyrosine-phosphorylating enzyme with sequence homology to serine/threonine kinases. Mol Cell Biol. 1991 Jan;11(1):568–572. doi: 10.1128/mcb.11.1.568. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Kandasamy M. K., Thorsness M. K., Rundle S. J., Goldberg M. L., Nasrallah J. B., Nasrallah M. E. Ablation of Papillar Cell Function in Brassica Flowers Results in the Loss of Stigma Receptivity to Pollination. Plant Cell. 1993 Mar;5(3):263–275. doi: 10.1105/tpc.5.3.263. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Kohorn B. D., Lane S., Smith T. A. An Arabidopsis serine/threonine kinase homologue with an epidermal growth factor repeat selected in yeast for its specificity for a thylakoid membrane protein. Proc Natl Acad Sci U S A. 1992 Nov 15;89(22):10989–10992. doi: 10.1073/pnas.89.22.10989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Krantz D. E., Zipursky S. L. Drosophila chaoptin, a member of the leucine-rich repeat family, is a photoreceptor cell-specific adhesion molecule. EMBO J. 1990 Jun;9(6):1969–1977. doi: 10.1002/j.1460-2075.1990.tb08325.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. 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]
  17. 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]
  18. Lopez J. A., Chung D. W., Fujikawa K., Hagen F. S., Papayannopoulou T., Roth G. J. Cloning of the alpha chain of human platelet glycoprotein Ib: a transmembrane protein with homology to leucine-rich alpha 2-glycoprotein. Proc Natl Acad Sci U S A. 1987 Aug;84(16):5615–5619. doi: 10.1073/pnas.84.16.5615. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. McFarland K. C., Sprengel R., Phillips H. S., Köhler M., Rosemblit N., Nikolics K., Segaloff D. L., Seeburg P. H. Lutropin-choriogonadotropin receptor: an unusual member of the G protein-coupled receptor family. Science. 1989 Aug 4;245(4917):494–499. doi: 10.1126/science.2502842. [DOI] [PubMed] [Google Scholar]
  20. Rothberg J. M., Jacobs J. R., Goodman C. S., Artavanis-Tsakonas S. slit: an extracellular protein necessary for development of midline glia and commissural axon pathways contains both EGF and LRR domains. Genes Dev. 1990 Dec;4(12A):2169–2187. doi: 10.1101/gad.4.12a.2169. [DOI] [PubMed] [Google Scholar]
  21. Schneider R., Schweiger M. A novel modular mosaic of cell adhesion motifs in the extracellular domains of the neurogenic trk and trkB tyrosine kinase receptors. Oncogene. 1991 Oct;6(10):1807–1811. [PubMed] [Google Scholar]
  22. 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]
  23. 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]
  24. 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]
  25. Stern D. F., Zheng P., Beidler D. R., Zerillo C. Spk1, a new kinase from Saccharomyces cerevisiae, phosphorylates proteins on serine, threonine, and tyrosine. Mol Cell Biol. 1991 Feb;11(2):987–1001. doi: 10.1128/mcb.11.2.987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Taylor S. S., Knighton D. R., Zheng J., Ten Eyck L. F., Sowadski J. M. Structural framework for the protein kinase family. Annu Rev Cell Biol. 1992;8:429–462. doi: 10.1146/annurev.cb.08.110192.002241. [DOI] [PubMed] [Google Scholar]
  27. 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]
  28. 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]
  29. 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]
  30. 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]
  31. Weinstein J. N., Blumenthal R., van Renswoude J., Kempf C., Klausner R. D. Charge clusters and the orientation of membrane proteins. J Membr Biol. 1982;66(3):203–212. doi: 10.1007/BF01868495. [DOI] [PubMed] [Google Scholar]
  32. von Heijne G. Patterns of amino acids near signal-sequence cleavage sites. Eur J Biochem. 1983 Jun 1;133(1):17–21. doi: 10.1111/j.1432-1033.1983.tb07424.x. [DOI] [PubMed] [Google Scholar]

Articles from The Plant Cell are provided here courtesy of Oxford University Press

RESOURCES