Post-translational Modifications in Plants

doi:10.1017/CBO9780511600401

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Walz, Alexander Park, Seijin Slovin, Janet P. Ludwig-Müller, Jutta Momonoki, Yoshie S. and Cohen, Jerry D. 2002. A gene encoding a protein modified by the phytohormone indoleacetic acid. Proceedings of the National Academy of Sciences, Vol. 99, Issue. 3, p. 1718.

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Agrawal, Ganesh Kumar and Rakwal, Randeep 2006. Rice proteomics: A cornerstone for cereal food crop proteomes. Mass Spectrometry Reviews, Vol. 25, Issue. 1, p. 1.

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Walz, Alexander Seidel, Claudia Rusak, Gordana Park, Seijin Cohen, Jerry D. and Ludwig-Müller, Jutta 2008. Heterologous expression of IAP1, a seed protein from bean modified by indole-3-acetic acid, in Arabidopsis thaliana and Medicago truncatula. Planta, Vol. 227, Issue. 5, p. 1047.

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Dashek, William V. 2017. Plant Cells and their Organelles. p. 42.

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Edited by N. H. Battey, University of Reading, H. G. Dickinson, University of Oxford, A. M. Hetherington, Lancaster University

Publisher:: Cambridge University Press
Online publication date:: July 2010
Print publication year:: 1993
Online ISBN:: 9780511600401
DOI:: https://doi.org/10.1017/CBO9780511600401

Subjects:: Plant Sciences, Life Sciences, Zoology, Molecular Biology, Biochemistry, and Structural Biology
Series:: Society for Experimental Biology Seminar Series (53)

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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.

‘… a good starting point for undergraduates, not only in terms of plant biology but also as a discussion of post translational modifications in general.’

David Stephens Source: FEBS Letters

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Post-translational Modifications in Plants

This Book has been cited by the following publications. This list is generated based on data provided by Crossref.

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Frontmatter
pp i-vi

Contents
pp vii-x

List of contributors
pp xi-xiv

List of abbreviations
pp xv-xviii

Preface
pp xix-xx

Some roles of post-translational modifications in plants
pp 1-16

Signal transduction and protein phosphorylation in bacteria
pp 17-38

Roles of protein phosphorylation in animal cells
pp 39-52

The significance of post-translational modification of proteins by phosphorylation in the regulation of plant development and metabolism
pp 53-64

Post-translational modification of chloroplast proteins and the regulation of protein turnover
pp 65-78

Purification of a small phosphoprotein from chloroplasts and characterisation of its phosphoryl group
pp 79-90

Use of synthetic peptides to study G proteins and protein kinases within plant cells
pp 91-108

Activation of membrane-associated protein kinase by lipids, its substrates, and its function in signal transduction
pp 109-122

Distribution and function of Ca2+-dependent, calmodulin-independent protein kinases
pp 123-148

Phosphorylation of the plasma membrane proton pump
pp 149-160

The regulation of phosphoenolpyruvate carboxylase by reversible phosphorylation
pp 161-170

Protein phosphorylation and circadian rhythms
pp 171-186

Control of translation by phosphorylation of mRNP proteins in Fucus and Xenopus
pp 187-196

Regulation of plant metabolism by reversible protein (serine/threonine) phosphorylation
pp 197-212

Detection, biosynthesis and some functions of glycans N-linked to plant secreted proteins
pp 213-242

Biosynthesis, intracellular transport and processing of ricin
pp 243-256

Post-translational processing of concanavalin A
pp 257-266

The role of cell surface glycoproteins in differentiation and morphogenesis
pp 267-284

Ubiquitination of proteins during floral development and senescence
pp 285-304

Index
pp 305-310

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Post-translational Modifications in Plants

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