Journal
JOURNAL OF BACTERIOLOGY
Volume 192, Issue 6, Pages 1719-1729Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JB.01429-09
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Funding
- National Institutes of Health [GM31030]
- MIT Center for Environmental Health Sciences [P30 ES002109]
- Centre National de la Recherche Scientifique
- Ministere de la Recherche et de l'Education Nationale
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The ubiquitous bacterial RNA-binding protein Hfq is involved in stress resistance and pathogenicity. In Sinorhizobium meliloti, Hfq is essential for the establishment of symbiosis with Medicago sativa and for nitrogen fixation. A proteomic analysis identifies 55 proteins with significantly affected expression in the hfq mutant; most of them are involved in cell metabolism or stress resistance. Important determinants of oxidative stress resistance, such as CysK, Gsh, Bfr, SodC, KatB, KatC, and a putative peroxiredoxine (SMc00072), are downregulated in the hfq mutant. The hfq mutant is affected for H2O2, menadione, and heat stress resistance. Part of these defects could result from the reductions of rpoE1, rpoE2, rpoE3, and rpoE4 expression levels in the hfq mutant. Some proteins required for efficient symbiosis are reduced in the hfq mutant, contributing to the drastic defect in nodulation observed in this mutant.
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