Skip to main content
SpringerLink
Log in

Two putative protein kinases from Arabidopsis thaliana contain highly acidic domains

  • Research Articles
  • Published:
Plant Molecular Biology Aims and scope Submit manuscript

Abstract

Two cDNA clones (ASK1 and ASK2) for plant protein kinases were cloned from Arabidopsis thaliana by screening cDNA libraries with a degenerate oligonucleotide probe that corresponds to a highly conserved motif among protein kinases. Sequence analysis shows that the clones contain open reading frames that encode 41.2 kDa (ASK1) and 40.1 kDa (ASK2) proteins, respectively. These coding regions contain all the conserved motifs of protein kinases. Structural analysis of the coding regions revealed that the two protein kinase genes share high sequence similarity to each other (76.6% identity). The catalytic domain located in the amino terminal region is most similar to the calcium/calmodulin-dependent protein kinase subfamily (47.2% to 54.2% similarity) and the SNF1 kinase subfamily (48.1% to 53.3% similarity). However, the carboxy terminal regions contain distinctive stretches of 21 (ASK1) and 19 (ASK2) acidic amino acids. These clones are the first report of protein kinases with such acidic amino acid regions. The transcripts of both genes are most abundant in leaf but are also expressed in other organs. The expression of the two genes is highly affected by light regime.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  1. Allen JF: How does protein phosphorylation regulates photosynthesis? Trends Biochem Sci 17: 12–17 (1992).

    Google Scholar 

  2. Aviv H, Leder P: Purification of biologically active globin messenger RNA by chromatography on oligothymidic acid cellulose. Proc Natl Acad Sci USA 69: 1408–1412 (1972).

    Google Scholar 

  3. Blowers DP, Morre DJ: Second messengers: Their existence and relationship to protein kinases. In: Boss WF, Morre DJ (eds) Second Messengers in Plant Growth and Development, pp. 1–28. Alan R. Liss, New York (1989).

    Google Scholar 

  4. Buddle RJA, Holbrook GP, Chollet R: Studies on the dark/light regulation of maize leaf pyruvate, orthophosphate dikinase by reversible phosphorylation. Arch Biochem Biophys 242: 283–290 (1985).

    Google Scholar 

  5. Celenza JL, Carlson M: A yeast gene that is essential for release from glucose repression encodes a protein kinase. Science 233: 1175–1180 (1986).

    Google Scholar 

  6. Church GM, Gilbert W: Genomic sequencing. Proc Natl Acad Sci USA 81: 1191–1195 (1984).

    Google Scholar 

  7. Cox HC, Goldberg RB: Analysis of plant gene expression. In: Show SH (ed) Plant Molecular Biology — A Practical Approach pp. 1–35. IRL Press, Oxford (1988).

    Google Scholar 

  8. Fliegel L, Burns K, MacLennan DH, Reithmeier RAF, Michalak M: Molecular cloning of the high affinity calcium-binding protein (calreticulin) of skeletal muscle sarcoplasmic reticulum. J Bicl Chem 264: 21522–21528 (1989).

    Google Scholar 

  9. Gilbert W, Marchionni M, McKnight G: On the antiquity of introns. Cell 46: 151–154 (1986).

    Google Scholar 

  10. Gomez-Marquez J, Segade F, Dosil M, Pichel JG, Bustelo XR, Freire M: The expression of prothymosin a gene in T lymphocytes and leukemic lymphoid cells is tied to lymphocyte proliferation. J Biol Chem 264: 8451–8454 (1989).

    Google Scholar 

  11. Gulber U, Hoffman BJ: A simple and very efficient method for generating cDNA libraries. Gene 25: 263–269 (1983).

    Google Scholar 

  12. Hanks SK: Homology probing: Identification of cDNA clones encoding members of protein-serine kinase family. Proc Natl Acad Sci USA 84: 388–392 (1987).

    Google Scholar 

  13. Hanks SK, Quinn AM, Hunter T: The protein kinase family: Conserved features and deduced phylogeny of the catalytic domains. Science 241: 42–52 (1988).

    Google Scholar 

  14. Harper JF, Sussman MR, Schaller GE, Putman-Evans C, Charbonneau H, Harmon AC: A calcium-dependent protein kinase with a regulatory domain similar to calmodulin. Science 252: 951–954 (1991).

    Google Scholar 

  15. Huber JLA, Huber SC, Nielsen TH: Protein phosphorylation as a mechanism for regulation of a spinach leaf sucrose-phosphate synthase activity. Arch Biochem Biophys 270: 681–690 (1989).

    Google Scholar 

  16. Joshi CP: An inspection of the domain between putative TATA box and translation start site in 79 plant genes. Nucl Acid Res 15: 6643–6653 (1987).

    Google Scholar 

  17. Klimczak KJ, Schindler U, Cashmore AR: DNA binding activity of the Arabidopsis G-box binding factor GBF-1 is stimulated by phosphorylation by casein kinase II from broccoli. Plant Cell 4: 87–98 (1992).

    Google Scholar 

  18. Lapeyre B, Bourbon H, Amalic F: Nucleolin, the major nuclear protein of growing eukaryotic cells: an unusual protein structure revealed by the nucleotide sequence. Proc Natl Acad Sci USA 84: 1472–1476 (1987).

    Google Scholar 

  19. Lathe R: Synthetic oligonucleotide probes deduced from amino acid sequence data theoretical and considerations. J Mol Biol 183: 1–12 (1985).

    Google Scholar 

  20. Lawton MA, Yamamoto RT, Hank SK, Lamb CJ: Molecular cloning of plant transcripts encoding protein kinase homologs. Proc Natl Acad Sci USA 86: 3140–3144 (1989).

    Google Scholar 

  21. Lin CR, Kapiloff MS, Durgerian S, Tatemoto K, Russo AF, Hanson P, Schulman H, Rosenfeld MG: Molecular cloning of a brain specific calcium/calmodulin-dependent protein kinase. Proc Natl Acad Sci USA 84: 5962–5966 (1987).

    Google Scholar 

  22. Lin X, Feng XH, Waston JC: Differential accumulation of transcripts encoding protein kinase homologs in greening pea seedlings. Proc Natl Acad Sci USA 88: 6951–6955 (1991).

    Google Scholar 

  23. Lindberg RA, Quinn AM, Hunter T: Dual-specificity kinases: will any hydroxyl do? Trends Biochem Sci 17: 114–119 (1992).

    Google Scholar 

  24. Martin FH, Castro MM, Fareed AE, Tinoco JRI: Base pairing involving deoxyinosine: Implication for probe design. Nucl Acid Res 13: 8927–8938 (1985).

    Google Scholar 

  25. Mizoguchi T, Hayashida N, Kazuo YS, Harada H, Kazuo S: Nucleotide sequence of a cDNA encoding a protein kinase homologue in Arabidopsis thaliana. Plant Mol Biol 18: 809–812 (1992).

    Google Scholar 

  26. Nimmo GA, Nimmo HG, Fewson CA, Wilkins MB: Diurnal changes in the properties of phosphoenolpyruvate carboxylase in Bryophyllum leaves: a possible covalent modification. FEBS Lett 178: 199–203 (1984).

    Google Scholar 

  27. Nishizuka Y: The molecular heterogeneity of protein kinase C and its implications for cellular regulation. Nature 334: 661–665 (1988).

    Google Scholar 

  28. Ohno S, Kawasaki H, Imajoh S, Suzuki K: Tissuespecific expression of three distinct types of rabbit protein kinase C. Nature 325: 161–166 (1987).

    Google Scholar 

  29. Polya GM, Chandra S, Chung R, Neumann GM, Hoj PB: Purification and characterization of wheat and pine small basic protein substrates for plant calcium-dependent protein kinase. Biochim Biophys Acta 1120: 273–280 (1992).

    Google Scholar 

  30. Proudfoot NJ, Brownlee GG: 3′ non-coding region sequences in eukaryotic messenger RNA. Nature 263: 211–214 (1976).

    Google Scholar 

  31. Ranjeva R, Boudet AM: Phosphorylation of proteins in plants: Regulatory effects and potential involvement in stimulus/response coupling. Annu Rev Plant Physiol 38: 73–93 (1987).

    Google Scholar 

  32. Rogers SO, Bendish AJ: Extraction of DNA from milligram amounts of fresh herbarium and minified plant tissues. Plant Mol Biol 5: 69–76 (1985).

    Google Scholar 

  33. Rubin PM, Randall DD: Regulation of plant pyruvate dehydrogenase complex by phosphorylation. Plant Physiol 60: 34–39 (1977).

    Google Scholar 

  34. Russel P, Nurse P: The mitotic inducer nim1+ functions in a regulatory network of protein kinase homologs controlling the initiation of mitosis. Cell 49: 569–576 (1987).

    Google Scholar 

  35. Sambrook J, Fritsch EF, Maniatis T: Molecular Cloning: A Laboratory Manual, 2nd ed. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY (1989).

    Google Scholar 

  36. Sanger F, Nicklen S, Coulson AR: DNA sequencing with chain termination inhibitors. Proc Natl Acad Sci USA 74: 5463–5467 (1977).

    Google Scholar 

  37. Shah DM, Hironaka CM, Wiegand RC, Harding EI, Kriv GG, Tiemeier DC: Structural analysis of a maize gene coding for glutathione-S-transferase involved in herbicide detoxification. Plant Mol Biol 6: 203–211 (1986).

    Google Scholar 

  38. Sorger PK, Pelham HR: The Glucose-regulated protein grp94 is related to heat shock protein hsp90. J Mol Biol 194: 341–344 (1987).

    Google Scholar 

  39. Spence MJ, Henzl MT, Lammers PJ: The structure of a Phaseolus vulgaris cDNA encoding the iron storage protein ferritin. Plant Mol Biol 17: 499–504 (1991).

    Google Scholar 

  40. Trewavas A, Gilroy S: Signal transduction in plant cells. Trends Genet 7: 356–361 (1991).

    Google Scholar 

  41. Vidal V, Ranty B, Dillenschneider M, Charpenteau M, Ranjeva R: Molecular characterization of a 70 kDa heat shock protein of bean mitochondria. Plant J 3: 143–150 (1993).

    Google Scholar 

  42. Walker JC, Zhang R: Relationship of a putative receptor protein kinase from maize to the S-locus glycoproteins of Brassica. Nature 345: 743–746 (1990).

    Google Scholar 

  43. Wen L, Huang Jk, Johnson BH, Reeck GR: A human placental cDNA clone that encodes nonhiston chromosomal protein HMG-1. Nucl Acid Res 17: 1197–1213 (1989).

    Google Scholar 

  44. Zocchi G: Phosphorylation/dephosphorylation of membrane proteins controls the mitochondrial proton-translocating ATPase activity on corn Zea mays roots. Plant Sci 40: 153–159 (1985).

    Google Scholar 

  45. Zorzato F, Fujii J, Otsu K, Phillips M, Green NM, Lai FA, Meissner G, MacLennan DH: Molecular cloning of cDNA encoding human and rabbit forms of the Ca2+ release channel (Ryanodine Receptor) of skeletal muscle sarcoplasmic reticulum. J Biol Chem 265: 2244–2256 (1990).

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Life Science, Pohang Institute of Science and Technology, 790-600, Pohang, Kyungbuk, South Korea

    Yu Shin Park, Suk Whan Hong, Sung Aeng Oh, June Myoung Kwak & Hong Gil Nam

  2. Department of Biology, Konkuk University, 133-701, Seoul, South Korea

    Yu Shin Park & Hyung Hoan Lee

  3. Plant Molecular Biology and Biotechnology Research Center, 660-701, Jinju, Kyungnam, South Korea

    June Myoung Kwak

Authors
  1. Yu Shin Park
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Suk Whan Hong
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Sung Aeng Oh
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. June Myoung Kwak
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Hyung Hoan Lee
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. Hong Gil Nam
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Park, Y.S., Hong, S.W., Oh, S.A. et al. Two putative protein kinases from Arabidopsis thaliana contain highly acidic domains. Plant Mol Biol 22, 615–624 (1993). https://doi.org/10.1007/BF00047402

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00047402

Key words

Search

Navigation