Proteomic analysis of Tunisian grapevine cultivar Razegui under salt stress

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 electrophoresis (2-DE) was used to analyze the proteo...

Ausführliche Beschreibung

Bibliographische Detailangaben
Veröffentlicht in:Journal of plant physiology. - 1979. - 165(2008), 5 vom: 07., Seite 471-81
1. Verfasser: Jellouli, Neila (VerfasserIn)
Weitere Verfasser: Ben Jouira, Hatem, Skouri, Houda, Ghorbel, Abdelwahed, Gourgouri, Ali, Mliki, Ahmed
Format: Aufsatz
Sprache:English
Veröffentlicht: 2008
Zugriff auf das übergeordnete Werk:Journal of plant physiology
Schlagworte:Journal Article Plant Proteins Proteome Sodium Chloride 451W47IQ8X
Beschreibung
Zusammenfassung: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 electrophoresis (2-DE) was used to analyze the proteome of the salt-tolerant Tunisian grapevine cultivar Razegui, subjected to a supply of 100mm NaCl over 15d. 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 pathogenesis-related (PR) protein 10 (V. vinifera). A full-length cDNA encoding the GP protein was isolated from grapevine salt-stressed leaves and sequenced. The predicted protein contained 158 amino acids and showed 98% identity with PR10 protein of of V. vinifera (accession no. Cac16165)
Beschreibung:Date Completed 21.07.2008
Date Revised 30.09.2020
published: Print-Electronic
Citation Status MEDLINE
ISSN:1618-1328