Plant Kinases Methods and Protocols
Modification of target protein properties by reversible phosphorylation events has been found to be one of the most prominent cellular control processes in all organisms. Recent advances in the areas of molecular biology and biochemistry are presenting ne
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Molecular Biology™
Series Editor John M. Walker School of Life Sciences University of Hertfordshire Hatfield, Hertfordshire, AL10 9AB, UK
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Plant Kinases Methods and Protocols
Edited by
Nico Dissmeyer Leibniz Institute of Plant Biochemistry (IPB), Halle (Saale), Germany
Arp Schnittger Institut de Biologie Moléculaire des Plantes Centre National de la Recherche Scientifique (IBMP-CNRS), Strasbourg, France
Editors Nico Dissmeyer, Ph.D. Leibniz Institute of Plant Biochemistry (IPB) Independent Junior Research Group on Protein Recognition and Degradation Weinberg 3, D-06120 Halle (Saale) Germany [email protected]
Arp Schnittger, Ph.D. Institut de Biologie Moléculaire des Plantes Centre National de la Recherche Scientifique (IBMP-CNRS) Unité Propre de Recherche 2357 12, rue du Général Zimmer F-67000 Strasbourg, France [email protected]
ISSN 1064-3745 e-ISSN 1940-6029 ISBN 978-1-61779-263-2 e-ISBN 978-1-61779-264-9 DOI 10.1007/978-1-61779-264-9 Springer New York Dordrecht Heidelberg London Library of Congress Control Number: 2011933668 © Springer Science+Business Media, LLC 2011 All rights reserved. This work may not be translated or copied in whole or in part without the written permission of the publisher (Humana Press, c/o Springer Science+Business Media, LLC, 233 Spring Street, New York, NY 10013, USA), except for brief excerpts in connection with reviews or scholarly analysis. Use in connection with any form of information storage and retrieval, electronic adaptation, computer software, or by similar or dissimilar methodology now known or hereafter developed is forbidden. The use in this publication of trade names, trademarks, service marks, and similar terms, even if they are not identified as such, is not to be taken as an expression of opinion as to whether or not they are subject to proprietary rights. Cover illustration: The title image is a collage of three different Arabidopsis thaliana plants. The endogenous activity of one of the major cell cycle kinases cyclin-dependent kinase A;1 (CDKA;1) increases from left to right. The two left individuals are cdka;1 homozygous null mutants that were partially complemented by phosphorylation-site substituted CDKA;1 variants and are compared to a wild type plant of the accession Columbia-0 on the right. The phosphosite mutants were expressed from the endogenous CDKA;1 promotor. The CDKA;1 variant on the left carries the double phospho-mimetic substitution T14D/Y15E in the ATP-binding pocket (P-loop) and that one in the center the single amino acid substitution T161D in the activation loop (T-loop). Both domains of CDKA;1 are required for catalysis and substitutions lead to a tremendous reduction in kinase activity. For reference, see Dissmeyer N. et al., Plant Cell (2007), Dissmeyer N. et al., Plant Cell (2009), and Chapter 6 of this book. Photographs by MAret-Linda Kalda, Max Planck Institute for Plant Breeding Research, Köln, Germany. Printed on aci
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