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- Title
Proteome phenotyping of Δ relA mutants in Enterococcus faecalis V583.
- Authors
Yan, Xue; Budin-Verneuil, Aurélie; Auffray, Yanick; Pichereau, Vianney
- Abstract
The (p)ppGpp synthetase RelA contributes to stress adaptation and virulence in Enterococcus faecalis V583. A 2-dimensional electrophoresis proteomic analysis of 2 relA mutants, i.e., Δ relA carrying a complete deletion of the relA gene, and Δ relAsp that is deleted from only its 3′ extremity, showed that 31 proteins were deregulated in 1 or both of these mutants. Mass spectrometry identification of these proteins showed that 10 are related to translation, including 5 ribosomal proteins, 3 proteins involved in translation elongation, and 2 proteins in tRNA synthesis; 14 proteins are involved in diverse metabolisms and biosynthesis (8 in sugar and energy metabolisms, 2 in fatty acid biosynthesis, 2 in amino acid biosynthesis, and 2 in nucleotide metabolism). Five proteins were relevant to the adaptation to different environmental stresses, i.e., SodA and a Dps family protein, 2 cold-shock domain proteins, and Ef1744, which is a general stress protein that plays an important role in the response to ethanol stress. The potential role of these proteins in the development of stress phenotypes associated with these mutations is discussed.
- Subjects
LIGASES; MICROBIAL virulence; ENTEROCOCCUS faecalis; PROTEOMICS; RIBOSOMAL proteins
- Publication
Canadian Journal of Microbiology, 2014, Vol 60, Issue 8, p525
- ISSN
0008-4166
- Publication type
Article
- DOI
10.1139/cjm-2014-0254