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

E. Campbell, R. Greenwell, J. Anthony, S. Wang, L. Lim, K. Das, H. Sofia, T. Donohue, S. Darst
Molecular cell. 2007 27:5 PubMed: 17803943

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.

Described groups:

  • ECF11

Cookies help us deliver our services. By using our services, you agree to our use of cookies. Learn more