1887

Abstract

Bacteria belonging to the Alphaproteobacteria normally harbour multiple copies of the heat shock sigma factor (known as σ, σ or RpoH). , a non-photosynthetic rhizobacterium, harbours five copies of genes, one of which is an homologue. The genes around the locus in show synteny with that found in rhizobia. The of was able to complement the temperature-sensitive phenotype of the mutant. Inactivation of in results in increased sensitivity to methylene blue and to triphenyl tetrazolium chloride (TTC). Exposure of to TTC and the singlet oxygen-generating agent methylene blue induced several-fold higher expression of . Comparison of the proteome of with its deletion mutant and with an strain overexpressing revealed chaperone GroEL, elongation factors (Ef-Tu and EF-G), peptidyl prolyl isomerase, and peptide methionine sulfoxide reductase as the major proteins whose expression was controlled by RpoH2. Here, we show that the RpoH2 sigma factor-controlled photooxidative stress response in is similar to that in the photosynthetic bacterium , but that RpoH2 is not involved in the detoxification of methylglyoxal in .

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2012-12-01
2024-04-25
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