Abstract
A cDNA clone for a receptor-like protein kinase gene (RPK1) was isolated from Arabidopsis thaliana. The clone is 1952 bp long with 1623 bp of an open reading frame encoding a peptide of 540 amino acids. The deduced peptide (RPK1) contains four distinctive domains characteristic of receptor kinases: (a) a putative amino-terminal signal sequence domain; (b) a domain with five extracellular leucine-rich repeat sequences; (c) a membrane-spanning domain; and (d) a cytoplasmic protein kinase domain that contains all of the 11 subdomains conserved among protein kinases. The RPK1 gene is expressed in flowers, stems, leaves, and roots. Expression of the RPK1 gene is induced within 1 h after treatment with abscisic acid (ABA). The gene is also rapidly induced by several environmental stresses such as dehydration, high salt, and low temperature, suggesting that the gene is involved in a general stress response. The dehydration-induced expression is not impaired in aba-1, abi1-1, abi2-1, and abi3-1 mutants, suggesting that the dehydration-induced expression of the RPK1 gene is ABA-independent. A possible role of this gene in the signal transduction pathway of ABA and the environmental stresses is discussed.
Full Text
The Full Text of this article is available as a PDF (2.5 MB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- 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]
- Dixon M. S., Jones D. A., Keddie J. S., Thomas C. M., Harrison K., Jones J. D. The tomato Cf-2 disease resistance locus comprises two functional genes encoding leucine-rich repeat proteins. Cell. 1996 Feb 9;84(3):451–459. doi: 10.1016/s0092-8674(00)81290-8. [DOI] [PubMed] [Google Scholar]
- Giraudat J., Parcy F., Bertauche N., Gosti F., Leung J., Morris P. C., Bouvier-Durand M., Vartanian N. Current advances in abscisic acid action and signalling. Plant Mol Biol. 1994 Dec;26(5):1557–1577. doi: 10.1007/BF00016490. [DOI] [PubMed] [Google Scholar]
- Godoy J. A., Lunar R., Torres-Schumann S., Moreno J., Rodrigo R. M., Pintor-Toro J. A. Expression, tissue distribution and subcellular localization of dehydrin TAS14 in salt-stressed tomato plants. Plant Mol Biol. 1994 Dec;26(6):1921–1934. doi: 10.1007/BF00019503. [DOI] [PubMed] [Google Scholar]
- Guerrero F. D., Jones J. T., Mullet J. E. Turgor-responsive gene transcription and RNA levels increase rapidly when pea shoots are wilted. Sequence and expression of three inducible genes. Plant Mol Biol. 1990 Jul;15(1):11–26. doi: 10.1007/BF00017720. [DOI] [PubMed] [Google Scholar]
- 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]
- Heckert L. L., Daley I. J., Griswold M. D. Structural organization of the follicle-stimulating hormone receptor gene. Mol Endocrinol. 1992 Jan;6(1):70–80. doi: 10.1210/mend.6.1.1738373. [DOI] [PubMed] [Google Scholar]
- Kobe B., Deisenhofer J. A structural basis of the interactions between leucine-rich repeats and protein ligands. Nature. 1995 Mar 9;374(6518):183–186. doi: 10.1038/374183a0. [DOI] [PubMed] [Google Scholar]
- 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]
- Lemmon M. A., Schlessinger J. Regulation of signal transduction and signal diversity by receptor oligomerization. Trends Biochem Sci. 1994 Nov;19(11):459–463. doi: 10.1016/0968-0004(94)90130-9. [DOI] [PubMed] [Google Scholar]
- Leung J., Bouvier-Durand M., Morris P. C., Guerrier D., Chefdor F., Giraudat J. Arabidopsis ABA response gene ABI1: features of a calcium-modulated protein phosphatase. Science. 1994 Jun 3;264(5164):1448–1452. doi: 10.1126/science.7910981. [DOI] [PubMed] [Google Scholar]
- Ma H. Protein phosphorylation in plants: enzymes, substrates and regulators. Trends Genet. 1993 Jul;9(7):228–230. doi: 10.1016/0168-9525(93)90075-s. [DOI] [PubMed] [Google Scholar]
- Meyer K., Leube M. P., Grill E. A protein phosphatase 2C involved in ABA signal transduction in Arabidopsis thaliana. Science. 1994 Jun 3;264(5164):1452–1455. doi: 10.1126/science.8197457. [DOI] [PubMed] [Google Scholar]
- Mizoguchi T., Irie K., Hirayama T., Hayashida N., Yamaguchi-Shinozaki K., Matsumoto K., Shinozaki K. A gene encoding a mitogen-activated protein kinase kinase kinase is induced simultaneously with genes for a mitogen-activated protein kinase and an S6 ribosomal protein kinase by touch, cold, and water stress in Arabidopsis thaliana. Proc Natl Acad Sci U S A. 1996 Jan 23;93(2):765–769. doi: 10.1073/pnas.93.2.765. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 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]
- Oh S. A., Lee S. Y., Chung I. K., Lee C. H., Nam H. G. A senescence-associated gene of Arabidopsis thaliana is distinctively regulated during natural and artificially induced leaf senescence. Plant Mol Biol. 1996 Feb;30(4):739–754. doi: 10.1007/BF00019008. [DOI] [PubMed] [Google Scholar]
- Park Y. S., Hong S. W., Oh S. A., Kwak J. M., Lee H. H., Nam H. G. Two putative protein kinases from Arabidopsis thaliana contain highly acidic domains. Plant Mol Biol. 1993 Jul;22(4):615–624. doi: 10.1007/BF00047402. [DOI] [PubMed] [Google Scholar]
- Park Y. S., Song O., Kwak J. M., Hong S. W., Lee H. H., Nam H. G. Functional complementation of a yeast vesicular transport mutation ypt1-1 by a Brassica napus cDNA clone encoding a small GTP-binding protein. Plant Mol Biol. 1994 Dec;26(6):1725–1735. doi: 10.1007/BF00019487. [DOI] [PubMed] [Google Scholar]
- Plana M., Itarte E., Eritja R., Goday A., Pagès M., Martínez M. C. Phosphorylation of maize RAB-17 protein by casein kinase 2. J Biol Chem. 1991 Nov 25;266(33):22510–22514. [PubMed] [Google Scholar]
- Skriver K., Mundy J. Gene expression in response to abscisic acid and osmotic stress. Plant Cell. 1990 Jun;2(6):503–512. doi: 10.1105/tpc.2.6.503. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Song W. Y., Wang G. L., Chen L. L., Kim H. S., Pi L. Y., Holsten T., Gardner J., Wang B., Zhai W. X., Zhu L. H. A receptor kinase-like protein encoded by the rice disease resistance gene, Xa21. Science. 1995 Dec 15;270(5243):1804–1806. doi: 10.1126/science.270.5243.1804. [DOI] [PubMed] [Google Scholar]
- 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]
- Stone J. M., Collinge M. A., Smith R. D., Horn M. A., Walker J. C. Interaction of a protein phosphatase with an Arabidopsis serine-threonine receptor kinase. Science. 1994 Nov 4;266(5186):793–795. doi: 10.1126/science.7973632. [DOI] [PubMed] [Google Scholar]
- Stone J. M., Walker J. C. Plant protein kinase families and signal transduction. Plant Physiol. 1995 Jun;108(2):451–457. doi: 10.1104/pp.108.2.451. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Straub P. F., Shen Q., Ho T. D. Structure and promoter analysis of an ABA- and stress-regulated barley gene, HVA1. Plant Mol Biol. 1994 Oct;26(2):617–630. doi: 10.1007/BF00013748. [DOI] [PubMed] [Google Scholar]
- Sun H., Tonks N. K. The coordinated action of protein tyrosine phosphatases and kinases in cell signaling. Trends Biochem Sci. 1994 Nov;19(11):480–485. doi: 10.1016/0968-0004(94)90134-1. [DOI] [PubMed] [Google Scholar]
- Torii K. U., Mitsukawa N., Oosumi T., Matsuura Y., Yokoyama R., Whittier R. F., Komeda Y. The Arabidopsis ERECTA gene encodes a putative receptor protein kinase with extracellular leucine-rich repeats. Plant Cell. 1996 Apr;8(4):735–746. doi: 10.1105/tpc.8.4.735. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Urao T., Katagiri T., Mizoguchi T., Yamaguchi-Shinozaki K., Hayashida N., Shinozaki K. Two genes that encode Ca(2+)-dependent protein kinases are induced by drought and high-salt stresses in Arabidopsis thaliana. Mol Gen Genet. 1994 Aug 15;244(4):331–340. doi: 10.1007/BF00286684. [DOI] [PubMed] [Google Scholar]
- Vilardell J., Martínez-Zapater J. M., Goday A., Arenas C., Pagès M. Regulation of the rab17 gene promoter in transgenic Arabidopsis wild-type, ABA-deficient and ABA-insensitive mutants. Plant Mol Biol. 1994 Feb;24(4):561–569. doi: 10.1007/BF00023554. [DOI] [PubMed] [Google Scholar]
- Walker J. C. Structure and function of the receptor-like protein kinases of higher plants. Plant Mol Biol. 1994 Dec;26(5):1599–1609. doi: 10.1007/BF00016492. [DOI] [PubMed] [Google Scholar]
- 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]
- 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]
- Yamaguchi-Shinozaki K., Shinozaki K. Characterization of the expression of a desiccation-responsive rd29 gene of Arabidopsis thaliana and analysis of its promoter in transgenic plants. Mol Gen Genet. 1993 Jan;236(2-3):331–340. doi: 10.1007/BF00277130. [DOI] [PubMed] [Google Scholar]