1. Response of the anaerobe Desulfovibrio vulgaris Hildenborough to oxidative conditions: proteome and transcript analysis
- Author
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Marjorie Fournier, Marie-Claire Durand, Zorah Dermoun, Alain Dolla, Danielle Moinier, Corinne Aubert, Interactions et Modulateurs de Réponses (IMR), Centre National de la Recherche Scientifique (CNRS), Institut de biologie structurale et microbiologie (IBSM), and Université de la Méditerranée - Aix-Marseille 2-Université Paul Cézanne - Aix-Marseille 3-Université de Provence - Aix-Marseille 1-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)
- Subjects
Proteome ,MESH: Glutaredoxins ,Oxidative phosphorylation ,medicine.disease_cause ,Biochemistry ,MESH: Peroxidases ,MESH: Gene Expression Profiling ,MESH: Desulfovibrio vulgaris ,Bacterial Proteins ,Glutaredoxin ,MESH: Anaerobiosis ,medicine ,Protein biosynthesis ,[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology ,Electrophoresis, Gel, Two-Dimensional ,MESH: Oxidoreductases ,Anaerobiosis ,Desulfovibrio vulgaris ,MESH: Bacterial Proteins ,Gene ,Glutaredoxins ,MESH: Oxidative Stress ,biology ,Gene Expression Profiling ,General Medicine ,Gel electrophoresis of proteins ,MESH: Electrophoresis, Gel, Two-Dimensional ,biology.organism_classification ,MESH: Proteome ,Oxidative Stress ,Peroxidases ,Oxidoreductases ,Oxidative stress - Abstract
International audience; The method of two-dimensional protein gel electrophoresis was used to evaluate the changes at the proteins level following oxygen exposure of the anaerobic sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough. Fifty-seven proteins showed significant differential expression. The cellular concentration of 35 proteins decreased while that of nineteen increased as a specific consequence of oxidative conditions. The proteins that were less abundant belonged to various functional categories such as nucleic acid and protein biosynthesis, detoxification mechanisms, or cell division. Interestingly, quantitative real-time PCR revealed that the genes encoding detoxification enzymes (rubrerythrins, superoxide reductase) are down regulated. The loss of viability of D. vulgaris Hildenborough under these oxidative conditions (Fournier et al., J. Biol. Chem. 279 (2004) 1785) can be directly related to the decrease in the cellular concentrations of these proteins, thereby specifying the toxicity of oxygen for the cells. Among the proteins that were more abundant under oxygen exposure, several thiol-specific peroxidases (thiol-peroxidase, BCP-like protein, and putative glutaredoxin) were identified. Using RT-PCR, the up-regulation of the genes encoding the thiol-peroxidase and the BCP was demonstrated. That is the first time that these proteins have been shown to be involved in the defense of D. vulgaris toward an oxidative stress. Several hypothetical proteins were also shown to be differentially expressed. A function in the defense mechanism against an oxidative stress is proposed for these uncharacterized proteins.
- Published
- 2005