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Title: A conserved structural module regulates transcriptional responses to diverse stress signals in bacteria

Journal Article · · Molecular Cell, 27(5):793-805
 [1];  [2];  [2];  [1];  [2];  [3];  [4];  [2];  [1]
  1. Rockefeller Univ., New York, NY (United States)
  2. Univ. of Wisconsin, Madison, WI (United States)
  3. Rutgers Univ., Piscataway, NJ (United States)
  4. Pacific Northwest National Lab. (PNNL), Richland, WA (United States)

In Rhodbacter sphaeroides, transcriptional response to singlet oxygen is controlled by the ECF (extracytoplasmic function) transcription factor, σΕ. ECF σ’s comprise the largest and most divergent group of the σ70-family members and are negatively regulated by their cognate anti-σ factor. Here, we determine the crystal structure of the Rhodobacter sphaeroides ECF σ factor, σE, in an inhibitory complex with its anti-σ, ChrR. The structure reveals that ChrR is composed of two structural domains separated by a flexible linker. The N-terminal domain sterically occludes the two primary binding determinants on σE for core RNA polymerase and is thus referred to as the ASD (anti-σ domain). Genetic and biochemical characterization of the two domains show that the ASD is sufficient to inhibit σE dependant transcription and the C-terminal domain is required for response to singlet oxygen and the release of σE from the ASD. In addition, structural and sequence analyses of the ASD of ChrR and other ECF anti-σ’s, reveal that the N-terminal domain of different groups of ECF anti-σ’s share a common structural fold with some sequence similarity. Bioinformatics studies show that the ASD occurs in as many as one third of ECF anti-σ’s, many of which have diverse C-terminal domains. The conserved ASD are sometimes fused to diverse C-terminal domains. These studies reveal that the ASD class of anti-σ’s are extraordinarily diverse, based on the type of σΕ factors they are associated with and the C-terminal domains to which they are linked.

Research Organization:
Pacific Northwest National Lab. (PNNL), Richland, WA (United States)
Sponsoring Organization:
USDOE
DOE Contract Number:
AC05-76RL01830
OSTI ID:
922886
Report Number(s):
PNNL-SA-52212; KJ0102000; TRN: US200803%%553
Journal Information:
Molecular Cell, 27(5):793-805, Vol. 27, Issue 5; ISSN 1097-2765
Country of Publication:
United States
Language:
English