A two-component phosphotransfer network involving ArcB, ArcA, and RssB coordinates synthesis and proteolysis of σ^S (RpoS) in <i>E. coli</i>

• Franziska Mika

• Regine Hengge

抄録

The general stress σ factor σ S (RpoS) in Escherichia coli is controlled at the levels of transcription, translation, and proteolysis. Here we demonstrate that the phosphorylated response regulator ArcA is a direct repressor of rpoS transcription that binds to two sites flanking the major rpoS promoter, with the upstream site overlapping an activating cAMP-CRP-binding site. The histidine sensor kinase ArcB not only phosphorylates ArcA, but also the σ S proteolytic targeting factor RssB, and thereby stimulates σ S proteolysis. Thus, ArcB/ArcA/RssB constitute a branched “three-component system”, which coordinates rpoS transcription and σ S proteolysis and thereby maintains low σ S levels in rapidly growing cells. We suggest that the redox state of the quinones, which controls autophosphorylation of ArcB, not only monitors oxygen but also energy supply, and we show that the ArcB/ArcA/RssB system is involved in σ S induction during entry into starvation conditions. Moreover, this induction is enhanced by a positive feedback that involves σ S -dependent induction of ArcA, which further reduces σ S proteolysis, probably by competing with RssB for residual phosphorylation by ArcB.

収録刊行物

• Genes & Development

  Genes & Development 19 (22), 2770-2781, 2005-11-15

  Cold Spring Harbor Laboratory

キーワード

• Developmental Biology
• Genetics

詳細情報

• CRID: 1361981468562325376
• NII論文ID: 30018918835
• DOI: 10.1101/gad.353705
• ISSN: 15495477
• ISSN: 08909369
• Web Site: https://syndication.highwire.org/content/doi/10.1101/gad.353705
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