The Escherichia coli σ(E)-dependent extracytoplasmic stress response is controlled by the regulated proteolysis of an anti-σ factor

Sarah E. Ades, Lynn E. Connolly, Benjamin M. Alba, Carol A. Gross

Research output: Contribution to journalArticlepeer-review

192 Scopus citations

Abstract

The activity of the stress-responsive σ factor, σ(E), is induced by the extracytoplasmic accumulation of misfolded or unfolded protein. The inner membrane protein RseA is the central regulatory molecule in this signal transduction cascade and acts as a σ(E)-specific anti-σ factor. Here we show that σ(E) activity is primarily determined by the ratio of RseA to σ(E). RseA is rapidly degraded in response to extracytoplasmic stress, leading to an increase in the free pool of σ(E) and initiation of the stress response. We present evidence that the putative inner membrane serine protease, DegS, is responsible for this regulated degradation of RseA.

Original languageEnglish (US)
Pages (from-to)2449-2461
Number of pages13
JournalGenes and Development
Volume13
Issue number18
DOIs
StatePublished - Sep 15 1999

All Science Journal Classification (ASJC) codes

  • Genetics
  • Developmental Biology

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