Skip to main content

Part of the book series: NATO ASI Series ((ASIAS,volume 104))

Abstract

The free calcium ion is now recognized as a major intracellular regulator of numerous biochemical and physiological processes in plants. Over the last six or seven years a large body of evidence has been accumulated which allows us to propose a working hypothesis for the mode of action of calcium-dependent mechanisms. This hypothesis consists of essentially three parts: (1) The free cytoplasmic calcium concentration is low (less than µM) and under metabolic control; (2) The cytoplasmic calcium concentration can be regulated by various extra- (or intra-) cellular signals; (3) The cytoplasmic calcium binds to receptor proteins (calmodulin beeing the most important one) which become activated and capable to modify enzyme or other activities. It is the aim of this review to put together all the essential information which supports our working hypothesis.

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

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 39.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 54.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Andrejauskas, E., Hertel, R., and Marmé, D., 1985, Specific binding of the calcium antagonist 3H-verapamil to membrane fractions from plants, J. Biol. Chem, 260: 5411–5414.

    CAS  Google Scholar 

  • Babu, Y. S., Sack, J. S., Greenhough, T. J., Bugg, C. E., Means, A. R., and Cook, W. J., 1985, Three-dimensional structure of calmodulin, Nature, 315: 37–40.

    Article  CAS  Google Scholar 

  • Dieter, P., and Marmé, D., 1980a, Partial purification of plant NAD kinase by calmodulin-Sepharose affinity chromatography, Cell Calcium, 1: 279–286.

    Article  CAS  Google Scholar 

  • Dieter, P., and Marmé, D., 1980b, Calmodulin-activated plant microsomal calcium uptake and purification of plant NAD kinase and other proteins by calmodulin-Sepharose affinity chromatography, Ann. N. Y. Acad. Sci, 356: 371–373.

    Article  CAS  Google Scholar 

  • Dieter, P., and Marmé, D., 1980c, Calcium transport in mitochondrial and microsomal fractions from higher plants, Planta, 150: 1–8.

    Article  CAS  Google Scholar 

  • Dieter, P., and Marmé, D., 1980d, Calmodulin activation of plant microsomal calcium uptake, Proc. Natl. Acad. Sci. USA, 77: 7311–7314.

    Article  CAS  Google Scholar 

  • Dieter, P., and Marme, D., 1981a, A calmodulin-dependent, microcomal ATPase from corn (Zea mays L.), FEBS Letters, 125: 245–248.

    Article  CAS  Google Scholar 

  • Dieter, P., and Marmé, D., 1981b, Far-red light irradiation of intact corn seedlings affects mitochondrial and calmodulin-dependent microsomal calcium transport, Biochem. Biophys. Res. Commun, 101: 749–755.

    Article  CAS  Google Scholar 

  • Dieter, P., and Marmé, D., 1983, The effect of calmodulin and far-red light on the kinetic properties of the mitochondrial and microsomal calcium ion transport system from corn, Planta, 159: 277–281.

    Article  CAS  Google Scholar 

  • Dieter, P., and Marmé, D., 1984, A calcium, calmodulin-dependent NAD kinase from corn is located in the outer mitochondrial membrane. J. Biol. Chem, 259: 184–189.

    CAS  Google Scholar 

  • Eldik van, L. J., and Watterson, D. M., 1985, Calmodulin structure and function, in: “Calcium and Cell Physiology”, D. Marme, ed., Springer, Heidelberg.

    Google Scholar 

  • Gross, J., 1982, Oxalate-enhanced active calcium uptake in membrane fractions from zucchini squash, in: “Plasmalemma and Tonoplast: Their Function in the Plant Cell”, D. Marmé, D. Marre, and R. Hertel, eds., Elsevier Biomedical Press, Amsterdam

    Google Scholar 

  • Hetherington, A., and Trewavas, A., 1982, Calcium-dependent protein kinase in pea shoot membranes, FEBS Letters, 145: 67–71.

    Article  CAS  Google Scholar 

  • Hetherington, A. M., and Trewavas, A., 1984, The regulation of membrane bound protein kinases by phospholipid and calcium, Ann. Proc. Phytochem. Soc. of Eur, 24: 181–197.

    Google Scholar 

  • Hodges, T. K., and Hanson, J. B., 1965, Calcium accumulation by maize mitochondria, PI. Physiol, 40: 101–108.

    Article  CAS  Google Scholar 

  • Kubowitz, B. P., Vanderhoef, L. N., and Hanson, J. B., 1982, ATP-dependent calbium transport in plasmalemma preparation from soybean hypocotyls, PI. Physiol, 69: 187–191.

    Article  Google Scholar 

  • Lukas, T. J., Iverson, D. B., Schleicher, M., and Watterson, D. M., 1984, Covalent structure of a higher plant calmodulin: Spinacea oleracea, Plant Physiol, 75: 788–795.

    Article  CAS  Google Scholar 

  • Marmé, D., and Dieter, P., 1983, The role of calcium and calmodulin in plants, in: “Calcium and Cell Function”, Vol. IV, Cheung, W. Y., ed., Academic Press, New York.

    Google Scholar 

  • Marmé, D., and Matzenauer, S., 1985, Protein kinase C and polyphosphoinositide metabolites: Their role in cellular signal transduction, in: “Calcium and Cell Physiology”, D. Marmé, ed., Springer, Heidelberg.

    Chapter  Google Scholar 

  • Means, A. R., Lagace, L., Simmen, R. C. M., and Putkey, J. A., 1985, Calmodulin gene structure and expression, in: “Calcium and Cell Physiology”, D. Marmé, ed., Springer, Heidelberg.

    Google Scholar 

  • Olah, Z., Berczi, A., and Erdei, L., 1983, Benzylaminopurine-induced coupling between calmodulin and Ca-ATP in wheat root microsomal membranes, FEBS Letters, 154: 395–399.

    Article  CAS  Google Scholar 

  • Polya, G. M., and Davies, J. R., 1982, Resolution of calcium-calmodulin-activated protein kinase from wheat germ, FEBS Letters, 150: 167–171

    Article  CAS  Google Scholar 

  • Ranjeva, Refeno, G., Boudet, A., and Marmé, D., 1983, Plant quinate: NAD+ oxidoreductase is activated by calcium-calmodulin-dependent phosphorylation, Proc. Nat. Acad. Sci. USA, 80: 5222–05224

    Article  CAS  Google Scholar 

  • Salimath, B. P., and Marmé, D., 1983, Protein phosphorylation and its regulation by calcium and calmodulin in membrane fractions from zucchini hypocotyls, Planta, 158: 560–568.

    Article  CAS  Google Scholar 

  • Schäfer, A., Bygrave, F., Matzenauer, S., and Marmé, D., 1985, Identification of a calcium and phospholipid-dependent protein kinase in plant tissue, FEBS Letters, in press.

    Google Scholar 

  • Simon, P., Bonzon, M., Greppin, H., and Marmé, D., 1984, Subchloroplastic localization of NAD kinase activity: evidence for a calcium, calmodu lin-dependent activity at the envelope and for a calcium, calmodulin dependent activity in the stroma of pea chloroplasts, FEBS Letters, 167: 332–338.

    Article  CAS  Google Scholar 

  • Tsien, R. Y., Pozzan, T., and Rink, T. J., 1982, Calcium homeostasis in intact lymphocytes: cytoplasmic free calcium monitored with a new intracellularly trapped fluorescent indicator, J. Cell Biol, 94: 325–334.

    Article  CAS  Google Scholar 

  • Williamson, R. E., 1981, Free calcium concentration in the cytoplasm: a regulator of plant cell function, What’s New Plant Physiol, 12: 45–48.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1986 Plenum Press, New York

About this chapter

Cite this chapter

Marmé, D. (1986). The Role of Calcium in the Regulation of Plant Metabolism. In: Trewavas, A.J. (eds) Molecular and Cellular Aspects of Calcium in Plant Development. NATO ASI Series, vol 104. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-2177-4_1

Download citation

  • DOI: https://doi.org/10.1007/978-1-4613-2177-4_1

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4612-9282-1

  • Online ISBN: 978-1-4613-2177-4

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics