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


ABSTRACT: A transcriptional response to singlet oxygen in Rhodobacter sphaeroides is controlled by the group IV sigma factor sigma(E) and its cognate anti-sigma ChrR. Crystal structures of the sigma(E)/ChrR complex reveal a modular, two-domain architecture for ChrR. The ChrR N-terminal anti-sigma domain (ASD) binds a Zn(2+) ion, contacts sigma(E), and is sufficient to inhibit sigma(E)-dependent transcription. The ChrR C-terminal domain adopts a cupin fold, can coordinate an additional Zn(2+), and is required for the transcriptional response to singlet oxygen. Structure-based sequence analyses predict that the ASD defines a common structural fold among predicted group IV anti-sigmas. These ASDs are fused to diverse C-terminal domains that are likely involved in responding to specific environmental signals that control the activity of their cognate sigma factor.

SUBMITTER: Campbell EA 

PROVIDER: S-EPMC2390684 | biostudies-literature | 2007 Sep

REPOSITORIES: biostudies-literature

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

Campbell Elizabeth A EA   Greenwell Roger R   Anthony Jennifer R JR   Wang Sheng S   Lim Lionel L   Das Kalyan K   Sofia Heidi J HJ   Donohue Timothy J TJ   Darst Seth A SA  

Molecular cell 20070901 5


A transcriptional response to singlet oxygen in Rhodobacter sphaeroides is controlled by the group IV sigma factor sigma(E) and its cognate anti-sigma ChrR. Crystal structures of the sigma(E)/ChrR complex reveal a modular, two-domain architecture for ChrR. The ChrR N-terminal anti-sigma domain (ASD) binds a Zn(2+) ion, contacts sigma(E), and is sufficient to inhibit sigma(E)-dependent transcription. The ChrR C-terminal domain adopts a cupin fold, can coordinate an additional Zn(2+), and is requi  ...[more]

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