Proteomic analysis of Tunisian grapevine cultivar Razegui under salt stress.pdf

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Proteomic analysis of Tunisian grapevine cultivar Razegui under salt stress.pdf

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Proteomic analysis of Tunisian grapevine cultivar Razegui under salt stress

ARTICLE IN PRESSJournal of Plant Physiology ] (]]]]) ]]]—]]]0176-1617/$ - s doi:10.1016/j. Abbreviation isoelectric focu polymerase cha transcription p 5-bromo-4-chlo Correspond E-mail addr 1Both author Please cite t Physiol (2007www.elsevier.de/jplphProteomic analysis of Tunisian grapevine cultivar Razegui under salt stress Neila Jelloulia,,1, Hatem Ben Jouiraa,1, Houda Skourib, Abdelwahed Ghorbela, Ali Gourgourib, Ahmed MlikiaaCBBC, Centre de Biotechnologie de Borj Cedria. Po.Box.901, Hammam-Lif 2050, Tunisia bCBS, Centre de Biotechnologie de Sfax, Tunisia Received 8 December 2006; received in revised form 22 February 2007; accepted 23 February 2007KEYWORDS Grapevine; PR10; Salt stress; Two-dimensional electrophoresisee front matter 2007 jplph.2007.02.009 s: 2-DE, two-dimensio sing; IPTG, isoploprl-b- in reaction; PR10.2, pa olymerase chain reactio ro-3-indoly-b-D-galacto ing author. Tel.: +216 79 ess: jel_neil@yahoo.fr s contributed equally t his article as: Jellouli N ), doi:10.1016/j.jplph.2Summary Salt stress is one of the major abiotic stresses in agriculture worldwide, especially in the Mediterranean area. We report here a proteomic approach to investigate the salt stress-responsive proteins in grapevine (Vitis vinifera). Two-dimensional electro- phoresis (2-DE) was used to analyze the proteome of the salt-tolerant Tunisian grapevine cultivar Razegui, subjected to a supply of 100mm NaCl over 15 d. Analysis of 2-DE gels derived from stressed plants revealed more than 800 reproducibly detected protein spots, with 48 proteins displaying a differential expression pattern, including 32 up-regulated, 9 down-regulated and 7 new protein spots induced after salt treatment. The presence of stress-responsive proteins in the different plant organs suggests that salt spreads systemically. Edman degradation analysis and database searching aided us in identifying a major protein GP. Database analysis revealed that this peptide has a 98% sequence similarity with a pathog