HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 276, Issue 23, 20300-20308, June 8, 2001

This Article Full Text Full Text (PDF) All Versions of this Article: 276/23/20300    most recent M009726200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Pierrugues, O. Articles by Kazmaier, M. Search for Related Content PubMed PubMed Citation Articles by Pierrugues, O. Articles by Kazmaier, M. Social Bookmarking                      What's this?

Lipid Phosphate Phosphatases in Arabidopsis
REGULATION OF THE AtLPP1 GENE IN RESPONSE TO STRESS^*

Olivier Pierrugues^§, Catherine Brutesco, June Oshiro^¶, Manolo Gouy, Yves Deveaux^**, George M. Carman^¶, Pierre Thuriaux, and Michael Kazmaier^§§

From  CEA/Cadarache, DSV-DEVM Laboratoire de Radiobiologie Végétale, 13108 Saint Paul-lez-Durance, France, the ^¶ Department of Food Science, Rutgers University, New Brunswick, New Jersey 08901, the  Laboratoire de Biométrie et Biologie Evolutive, UMR CNRS 5558, Université C, Bernard-Lyon 1, 69622 Villeurbanne, and  CEA/Saclay, DSV-Service de Génétique et de Biologie Moléculaire, 91108 Gif-sur-Yvette, France

An Arabidopsis thaliana gene (AtLPP1) was isolated on the basis that it was transiently induced by ionizing radiation. The putative AtLPP1 gene product showed homology to the yeast and mammalian lipid phosphate phosphatase enzymes and possessed a phosphatase signature sequence motif. Heterologous expression and biochemical characterization of the AtLPP1 gene in yeast showed that it encoded an enzyme (AtLpp1p) that exhibited both diacylglycerol pyrophosphate phosphatase and phosphatidate phosphatase activities. Kinetic analysis indicated that diacylglycerol pyrophosphate was the preferred substrate for AtLpp1p in vitro. A second Arabidopsis gene (AtLPP2) was identified based on sequence homology to AtLPP1 that was also heterologously expressed in yeast. The AtLpp2p enzyme also utilized diacylglycerol pyrophosphate and phosphatidate but with no preference for either substrate. The AtLpp1p and AtLpp2p enzymes showed differences in their apparent affinities for diacylglycerol pyrophosphate and phosphatidate as well as other enzymological properties. Northern blot analyses showed that the AtLPP1 gene was preferentially expressed in leaves and roots, whereas the AtLPP2 gene was expressed in all tissues examined. AtLPP1, but not AtLPP2, was regulated in response to various stress conditions. The AtLPP1 gene was transiently induced by genotoxic stress (gamma ray or UV-B) and elicitor treatments with mastoparan and harpin. The regulation of the AtLPP1 gene in response to stress was consistent with the hypothesis that its encoded lipid phosphate phosphatase enzyme may attenuate the signaling functions of phosphatidate and/or diacylglycerol pyrophosphate that form in response to stress in plants.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				Y. Nakamura, M. Tsuchiya, and H. Ohta Plastidic Phosphatidic Acid Phosphatases Identified in a Distinct Subfamily of Lipid Phosphate Phosphatases with Prokaryotic Origin J. Biol. Chem., September 28, 2007; 282(39): 29013 - 29021. [Abstract] [Full Text] [PDF]

				C. Zalejski, S. Paradis, R. Maldiney, Y. Habricot, E. Miginiac, J.-P. Rona, and E. Jeannette Induction of Abscisic Acid-Regulated Gene Expression by Diacylglycerol Pyrophosphate Involves Ca2+ and Anion Currents in Arabidopsis Suspension Cells Plant Physiology, August 1, 2006; 141(4): 1555 - 1562. [Abstract] [Full Text] [PDF]

				C. Xu, J. Fan, J. E. Froehlich, K. Awai, and C. Benning Mutation of the TGD1 Chloroplast Envelope Protein Affects Phosphatidate Metabolism in Arabidopsis PLANT CELL, November 1, 2005; 17(11): 3094 - 3110. [Abstract] [Full Text] [PDF]

				A. Marmagne, M.-A. Rouet, M. Ferro, N. Rolland, C. Alcon, J. Joyard, J. Garin, H. Barbier-Brygoo, and G. Ephritikhine Identification of New Intrinsic Proteins in Arabidopsis Plasma Membrane Proteome Mol. Cell. Proteomics, July 1, 2004; 3(7): 675 - 691. [Abstract] [Full Text] [PDF]

				G.-S. Han, C. N. Johnston, and G. M. Carman Vacuole Membrane Topography of the DPP1-encoded Diacylglycerol Pyrophosphate Phosphatase Catalytic Site from Saccharomyces cerevisiae J. Biol. Chem., February 13, 2004; 279(7): 5338 - 5345. [Abstract] [Full Text] [PDF]