JXB Advance Access published online on April 4, 2006
Journal of Experimental Botany, doi:10.1093/jxb/erj162
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1 Laboratoire de Physiologie Cellulaire Végétale, UMR 5168 CEA/CNRS/INRA/Université Joseph Fourier, CEA-Grenoble, F-38054 Grenoble-cedex 9, France
* To whom correspondence should be addressed. Proteomics is a very powerful approach to link the information contained in sequenced genomes, like that of Arabidopsis, to the functional knowledge provided by studies of plant cell compartments. This article summarizes the different steps of a versatile strategy that has been developed to decipher plant membrane proteomes. Initiated with envelope membranes from spinach chloroplasts, this strategy has been adapted to thylakoids, and further extended to a series of membranes from the model plant Arabidopsis: chloroplast envelope membranes, plasma membrane, and mitochondrial membranes. The first step is the preparation of highly purified membrane fractions from plant tissues. The second step in the strategy is the fractionation of membrane proteins on the basis of their physico-chemical properties. Chloroform/methanol extraction and washing of membranes with NaOH, NaCl or any other agent led to the simplification of the protein content of the fraction to be analysed. The next step is the genuine proteomic step, i.e. the separation of proteins by 1D-gel electrophoresis followed by in-gel proteolytic digestion of the polypeptides, analysis of the proteolytic peptides using mass spectrometry, and protein identification by searching through databases. The last step is the validation of the procedure by checking the subcellular location. The results obtained by using this strategy demonstrate that a combination of different proteomics approaches, together with bioinformatics, indeed provide a better understanding of the biochemical machinery of the different plant membranes at the molecular level.
Received April 10, 2005
Accepted February 15, 2006
Plant Proteomics Special Issue Article
A versatile method for deciphering plant membrane proteomes
Norbert Rolland 1,
Myriam Ferro 2,
Geneviève Ephritikhine 3,
Anne Marmagne 3,
Claire Ramus 2,
Sabine Brugière 2,
Daniel Salvi 1,
Daphné Seigneurin-Berny 1,
Jacques Bourguignon 1,
Hélène Barbier-Brygoo 3,
Jacques Joyard 1 *,
and
Jérome Garin 2
2 Laboratoire de Chimie des Protéines, ERM-0201 INSERM/CEA, CEA-Grenoble, F-38054 Grenoble-cedex 9, France
3 Institut des Sciences du Végétal, UPR 2355, CNRS, F-91198 Gif sur Yvette-cedex, France
Jacques Joyard, E-mail: jacques.joyard{at}cea.fr
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