Post-translational modifications in plants

Author(s)

• Battey, N. H.
• Dickinson, Hugh G.
• Hetherington, A. M.

Bibliographic Information

Post-translational modifications in plants

edited by N.H. Battey, H.G. Dickinson, A.M. Hetherington

（Seminar series / Society for Experimental Biology, 53）

Cambridge University Press, 1993

Note

Papers from a symposium held at Lancaster in April 1992

Includes bibliographical references and index

Description and Table of Contents

Description

Post-translational modifications are now known to play a fundamental role in regulating the activity, location and function of a wide range of proteins. In plant cells work on different types of post-translational modifications has progressed largely along independent lines. This book brings research workers together to allow an exchange of ideas, and reflects a diversity of interest whilst also revealing common ground. An introductory chapter reviewing recent progress in the field is followed by reviews of protein phosphorylation in bacteria and animals which provide a useful perspective on this subject in plants. Consideration is then given to plant protein kinases and the processes they control. Acylation and glycosylation, and their functions in protein targeting and folding are reviewed, along with the roles of glycoproteins in plant development and of ubiquitination in plant senescence.

Table of Contents

• 1. Some roles of post-translational modifications in plants N. H. Battey
• 2. Signal transduction and protein phosphorylation in bacteria R. A. Dixon
• 3. Roles of protein phosphorylation in animal cells D. G. Hardie
• 4. The significance of post-translational modification of proteins by phosphorylation in the regulation of plant development and metabolism K. M. Fallon and A. J. Trewavas
• 5. Post-translational modification of chloroplast proteins and the regulation of protein turnover A. K. Mattoo
• 6. Purification of a small phosphoprotein from chloroplasts and characterisation of its phosphoryl group J. Soll
• 7. Use of synthetic peptides to study G-proteins and protein kinases within plant cells I. R. White
• 8. Activation of membrane-associated protein kinase by lipids, its substrates, and its function in signal transduction G. F. E. Scherer
• 9. Distribution and function of Ca2+-dependent, calmodulin-independent protein kinases N. H. Battey
• 10. Phosphorylation of the plasma membrane proton pump M. R. Sussman
• 11. The regulation of phosphoenolpyruvate carboxylase by reversible phosphorylation H. G. Nimmo
• 12. Protein phosphorylation and circadian rhythms L. Rensing
• 13. Control of translation by phosphorylation of mRNP proteins in Fucus and Xenopus A. D. Shirras
• 14. Regulation of plant metabolism by reversible protein (serine/threonine) phosphorylation R. W. Mackintosh and C. Mackintosh
• 15. Detection, biosynthesis and some functions of glycans N-linked to plant secreted proteins L. Faye: 16. Biosynthesis, intracellular transport and processing of ricin J. M. Lord and L. M. Roberts
• 17. Post-translational processing of concanavalin D. Bowles
• 18. The role of cell surface glycoproteins in differentiation and morphogenesis J. P. Knox.

by "Nielsen BookData"

Details

• NCID: BA20052769
• ISBN:
  • 0521411815
• LCCN: 92028694
• Country Code: uk
• Title Language Code: eng
• Text Language Code: eng
• Place of Publication: Cambridge [England] ; New York, NY,
• Pages/Volumes: xx, 310 p.
• Size: 24 cm
• Classification:
  • LCC : QK898.P8
  • DC20 : 581.19/296
• Subject Headings:
  • LCSH : Post-translational modification -- Congresses
  • LCSH : Plant proteins -- Synthesis -- Congresses
• Parent Bibliography ID:
  • BA00368351