Skip to main content
Log in

Rice calcium-dependent protein kinase isoforms OsCDPK2 and OsCDPK11 show different responses to light and different expression patterns during seed development

  • Published:
Plant Molecular Biology Aims and scope Submit manuscript

Abstract

We investigated the spatial and temporal expression patterns of two rice calcium-dependent protein kinases (CDPKs), OsCDPK2 and OSCDPK11, using isoform-specific antisera. Bands of the expected molecular sizes for OsCDPK2 (59 kDa) and OsCDPK11 (61 kDa) were detected on western blots. OsCDPK2 and OsCDPK11 mRNA and protein levels increased in unison during flower development. However, at the onset of seed development, the protein expression profiles diverged significantly. OsCDPK2 protein was expressed at low levels during early seed development, but increased to high levels that were maintained in later stages (20 days after fertilisation, DAF). Conversely, OsCDPK11 protein levels were high at the beginning of seed development, but fell rapidly from 10 DAF onwards. This decrease in the level of OsCDPK11 protein was associated with the abundant synthesis of a truncated mRNA species. OsCDPK2 expression was also closely associated with light perception. OsCDPK2 protein was barely detectable in green leaves exposed to light, but levels increased sharply when plants were shifted to darkness. Initially, this increase reflected a rapid elevation in the levels of OsCDPK2 mRNA, which was normally located in the mesophyll. Conversely, OsCDPK11 mRNA and protein levels were unaffected by light. These data strongly indicate that two rice CDPK isoforms have different functions in seed development and in response to light in leaves.

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

Access this article

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

Instant access to the full article PDF.

Similar content being viewed by others

References

  • Abo-El-Saad, M. and Wu, R. 1995. A rice membrane calcium-dependent protein kinase is induced by gibberelin. Plant Physiol. 108: 787–793.

    PubMed  Google Scholar 

  • Ausubel, F.M., Brent, R., Kingston, R.E., Moore, D.D., Seidman, J.G., Smith, J.A. and Struhl, K. 1992. Short Protocols in Molec-ular Biology, 2nd ed., Greene Publishing Associates/John Wiley, New York.

    Google Scholar 

  • Bachmann, M., Shiraishi, N., Campbell, W.H., Yoo, B.C., Harmon, A.C. and Huber, S.C. 1996. Identification of Ser-543 as the major regulatory phosphorylation site in spinach leaf nitrate reductase. Plant Cell 8: 505–517.

    PubMed  Google Scholar 

  • Binder, B.M., Harper, J.F. and Sussman, M.R. 1994. Characteriza-tion of an Arabidopsis calmodulin-like domain protein kinase pu-rified from Escherichia coli using an affinity sandwich technique. Biochemistry 33: 2033–2041.

    PubMed  Google Scholar 

  • Botella, J.R., Arteca, J.M., Somodevilla, M. and Arteca, R.N. 1996. Calcium-dependent protein kinase gene expression in response to physical and chemical stimuli in mungbean (Vigna radiata). Plant Mol. Biol. 30: 1129–1137.

    PubMed  Google Scholar 

  • Breviario, D., Morello, L. and Gianì, S. 1995. Molecular cloning of two novel rice cDNA sequences encoding putative calcium-dependent protein kinases. Plant Mol. Biol. 27: 953–967.

    PubMed  Google Scholar 

  • Cañas, L.A., Busscher, M., Angenent, G.C., Beltran, J.P. and van Tunen, A.J. 1994. Nuclear localization of the petunia MADS box protein FBP1. Plant J. 6: 597–604.

    Google Scholar 

  • Douglas, P. Moorhead, G., Hong, Y., Morrice, N. and MacKintosh, C. 1998. Purification of a nitrate reductase kinase from Spinacea oleracea leaves, and its identification as a calmodulin-domain protein kinase. Planta 206: 435–442.

    PubMed  Google Scholar 

  • Estruch, J.J., Kadwell, S., Merlin, E. and Crossland, L. 1994. Cloning and characterization of a maize pollen-specific calcium-dependent calmodulin-independent protein kinase. Proc. Natl. Acad. Sci. USA 91: 8837–8841.

    PubMed  Google Scholar 

  • Furumoto, T., Ogawa, N., Hata, S. and Izui, K. 1996. Plant calcium-dependent protein kinase-related kinases (CRKs) do not require calcium for their activities. FEBS Lett. 396: 147–151.

    PubMed  Google Scholar 

  • Gianì, S., Qin, X., Faoro, F. and Breviario, D. 1998. In rice, oryzalin and abscisic acid differentially affect tubulin mRNA and protein levels. Planta 205: 334–341.

    PubMed  Google Scholar 

  • Harmon, A.C., Putnam-Evans, C. and Cormier, M.J. 1987. A calcium-dependent but calmodulin-independent protein kinase from soybean. Plant Physiol. 83: 830–837.

    Google Scholar 

  • Harmon, A.C., Yoo, B.C. and McCaffery, C. 1994. Pseudosubstrate inhibition of CDPK, a protein kinase with a calmodulin-like domain. Biochemistry 33: 7278–7287.

    PubMed  Google Scholar 

  • Harper, J.F., Sussman, M.R., Schaller, G.E., Putnam-Evans, C., Charbonneau, H. and Harmon, A.C. 1991. A calcium-dependent protein kinase with a regulatory domain similar to calmodulin. Science 252: 951–954.

    PubMed  Google Scholar 

  • Harper, J.F., Binder, B.M. and Sussman, M.R. 1993. Calcium and lipid regulation of an Arabidopsis protein kinase expressed in Escherichia coli. Biochemistry 32: 3282–3290.

    PubMed  Google Scholar 

  • Harper, J.F., Huang, J.F. and Lloyd, S.J. 1994. Genetic identification of an autoinhibitor in CDPK, a protein kinase with a calmodulin-like domain. Biochemistry 33: 7267–7277.

    PubMed  Google Scholar 

  • Hong, Y., Takano, M., Liu, C.M., Gasch, A., Chye, M.L. and Chua, N.H. 1996. Expression of three members of the calcium-dependent protein kinase gene family in Arabidopsis thaliana. Plant Mol. Biol. 30: 1259–1275.

    PubMed  Google Scholar 

  • Hrabak, E.M., Dickmann, I.J., Satterlee, J.S. and Sussman, M.R. 1996. Characterization of eight new members of the calmodulin-like domain protein kinase gene family from Arabidopsis thaliana. Plant Mol. Biol. 31: 405–412.

    PubMed  Google Scholar 

  • Huang, J.F., Teyton, L. and Harper, J.F. 1996. Activation of a Ca 2 C-dependent protein kinase involves intramolecular bind-ing of a calmodulin-like regulatory domain. Biochemistry 35: 13222–13230.

    PubMed  Google Scholar 

  • Johnson, K.D. and Chrispeels, M.J. 1992. Tonoplast-bound protein kinase phosphorylates tonoplast intrinsic protein. Plant Physiol. 100: 1787–1795.

    Google Scholar 

  • Kawasaki, T., Hayashida, N., Baba, T., Shinozaki, K. and Shimada, H. 1993. The gene encoding a calcium-dependent protein kinase located near the sbeI gene encoding starch branching enzyme I is specifically expressed in developing rice seeds. Gene 129: 183–189.

    Google Scholar 

  • Krysan, P.J., Young, J.C., Tax, F. and Sussman, M.R. 1996. Identifi-cation of transferred DNA insertions within Arabidopsis genes involved in signal transduction and ion transport. Proc. Natl. Acad. Sci. USA 93: 8145–8150.

    PubMed  Google Scholar 

  • Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680–685.

    PubMed  Google Scholar 

  • Lee, J.Y., Yoo, B.C. and Harmon, A.C. 1998. Kinetic and calcium-binding properties of three calcium-dependent protein kinase isoenzymes from soybean. Biochemistry 37: 6801–6809.

    PubMed  Google Scholar 

  • Li, J., Lee, Y.R.J. and Assmann, S.M. 1998. Guard cells possess a calcium-dependent protein kinase that phosphorylates the KAT1 potassium channel. Plant Physiol. 116: 785–795.

    PubMed  Google Scholar 

  • Lindzen, E. and Choi, J.H. 1995. A carrot cDNA encoding an atypical protein kinase homologous to plant calcium-dependent protein kinases. Plant Mol. Biol. 28: 785–797.

    PubMed  Google Scholar 

  • Lino, B., Baizabal-Aguirre, V.M. and Gonzalez de la Vara, L.E. 1998. The plasma-membrane H C-ATPase from beet root is in-hibited by a calcium-dependent phosphorylation. Planta 204: 352–359.

    PubMed  Google Scholar 

  • Lowry, O.H., Rosenbrough, N.J., Farr, A.L. and Randall, R.J. 1951. Protein measurement with the Folin phenol regent. J. Biol. Chem. 193: 265–275.

    PubMed  Google Scholar 

  • Pei, Z.M., Ward, J.M., Harper, J.F. and Schroeder, J.I. 1996. A novel chloride channel in Vicia faba guard cell vacuoles activated by the serine/threonine kinase, CDPK. EMBO J. 15: 6564–6574.

    Google Scholar 

  • Rechsteiner, M. and Rogers, S.W. 1996. PEST sequences and regulation by proteolysis. Trends Biochem. Sci. 21: 267–271.

    PubMed  Google Scholar 

  • Roberts, D.M. and Harmon, A.C. 1992. Calcium-modulated pro-teins: targets of intracellular calcium signals in higher plants. Annu. Rev. Plant Physiol. Plant Mol. Biol. 43: 375–414.

    Google Scholar 

  • Saijo, Y., Hata, S., Sheen, J. and Izui, K. 1997. cDNA cloning and procaryotic expression of maize calcium-dependent protein kinase. Biochim. Biophys. Acta. 1350: 109–114.

    PubMed  Google Scholar 

  • Satterlee, J.S. and Sussman, M.R. 1998. Unusual membrane-associated protein kinases in higher plants. J. Membrane Biol. 164: 205–213.

    Google Scholar 

  • Schaller, J.E. and Sussman, M.R. 1988. Phosphorylation of the plasma-membrane H C-ATPase of oat roots by a calcium-stimulated protein kinase. Planta 173: 509–518.

    Google Scholar 

  • Schaller, G.E., Harmon, A.C. and Sussman, M.R. 1992. Char-acterization of a calcium-and lipid-dependent protein kinase associated with the plasma membrane of oat. Biochemistry 31: 1721–1727.

    PubMed  Google Scholar 

  • Sheen, J. 1996. Ca 2 C-dependent protein kinases and stress signal transduction in plants. Science 274: 1900–1902.

    PubMed  Google Scholar 

  • Stone, J.M. and Walker, J.C. 1995. Plant protein kinase families and signal transduction. Plant Physiol. 108: 451–457.

    PubMed  Google Scholar 

  • Tahtiharju, S., Sangwan, V., Monroy, A.F., Dhindsa, R.S. and Borg, M. 1997. The induction of kin genes in cold-acclimating Ara-bidopsis thaliana. Evidence of a role for calcium. Planta 203: 442–447.

    PubMed  Google Scholar 

  • Takezawa, D., Patil, S., Bhatia, A. and Poovaiah, B.W. 1996. Calcium-dependent protein kinase genes in corn roots. J. Plant Physiol. 149: 329–335.

    PubMed  Google Scholar 

  • Urao, T., Katigiri, T., Mizoguchi, T., Yamaguchi-Shinozaki, K., Hayashida, N. and Shinozaki, K. 1994. Two genes that encode Ca 2 C-dependent protein kinases are induced by drought and high-salt stresses in Arabidopsis thaliana. Mol. Gen. Genet. 244: 331–340.

    PubMed  Google Scholar 

  • Vierstra, R.D. 1996. Proteolysis in plants: mechanisms and func-tions. Plant Mol. Biol. 32: 275–302.

    PubMed  Google Scholar 

  • Weaver, C.D. and Roberts, D.M. 1992. Determination of the site of phosphorylation of nodulin 26 by the calcium-dependent protein kinase from soybean nodules. Biochemistry 31: 8954–8959.

    PubMed  Google Scholar 

  • Yoo, B.C. and Harmon, A.C. 1996. Intramolecular binding con-tributes to the activation of CDPK, a protein kinase with a calmodulin-like domain. Biochemistry 35: 12029–12037.

    PubMed  Google Scholar 

  • Zhang, X.O. and Chollet, R. 1997. Seryl-phosphorylation of soybean nodule sucrose synthase (nodulin-100) by a Ca 2 C-dependent protein kinase. FEBS Lett. 410: 126–130.

    PubMed  Google Scholar 

  • Zhao, Y., Pokutta, S., Maurer, P., Lindt, M., Franklin, R.M. and Kappes, B. 1994. Calcium-binding properties of a calcium-dependent protein kinase from Plasmodium falciparum and the significance of individual calcium-binding sites for kinase acti-vation. Biochemistry 33: 3714–3721.

    PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Frattini, M., Morello, L. & Breviario, D. Rice calcium-dependent protein kinase isoforms OsCDPK2 and OsCDPK11 show different responses to light and different expression patterns during seed development. Plant Mol Biol 41, 753–764 (1999). https://doi.org/10.1023/A:1006316422400

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1023/A:1006316422400

Navigation