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Crystal structure of the Bacillus subtilis anti-alpha, global transcriptional regulator, Spx, in complex with the alpha C-terminal domain of RNA polymerase.

Publication ,  Journal Article
Newberry, KJ; Nakano, S; Zuber, P; Brennan, RG
Published in: Proc Natl Acad Sci U S A
November 1, 2005

Spx, a global transcription regulator in Bacillus subtilis, interacts with the C-terminal domain of the alpha subunit (alphaCTD) of RNA polymerase to control gene expression under conditions of disulfide stress, which is sensed by disulfide bond formation between Spx residues C10 and C13. Here, we describe the crystal structure of the B. subtilis alphaCTD bound to oxidized Spx. Analysis of the complex reveals interactions between three regions of "anti-alpha" Spx and helix alpha1 and the "261" determinant of alphaCTD. The former contact could disrupt the interaction between alphaCTD and activator proteins or alter the DNA-bound conformation of alphaCTD, thereby repressing activator-stimulated transcription. Binding to the 261 determinant would prevent interaction between alphaCTD and region 4 of sigma(A). Intriguingly, the Spx disulfide bond is far from the alphaCTD-Spx interface, suggesting that Spx regulates transcription allosterically or through the redox-dependent creation or destruction of binding sites for additional components of the transcription machinery.

Duke Scholars

Published In

Proc Natl Acad Sci U S A

DOI

ISSN

0027-8424

Publication Date

November 1, 2005

Volume

102

Issue

44

Start / End Page

15839 / 15844

Location

United States

Related Subject Headings

  • Transcription, Genetic
  • Repressor Proteins
  • Protein Structure, Tertiary
  • Protein Binding
  • Oxidation-Reduction
  • Gene Expression Regulation, Bacterial
  • DNA-Directed RNA Polymerases
  • Crystallization
  • Binding Sites
  • Bacterial Proteins
 

Citation

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Newberry, K. J., Nakano, S., Zuber, P., & Brennan, R. G. (2005). Crystal structure of the Bacillus subtilis anti-alpha, global transcriptional regulator, Spx, in complex with the alpha C-terminal domain of RNA polymerase. Proc Natl Acad Sci U S A, 102(44), 15839–15844. https://doi.org/10.1073/pnas.0506592102
Newberry, Kate J., Shunji Nakano, Peter Zuber, and Richard G. Brennan. “Crystal structure of the Bacillus subtilis anti-alpha, global transcriptional regulator, Spx, in complex with the alpha C-terminal domain of RNA polymerase.Proc Natl Acad Sci U S A 102, no. 44 (November 1, 2005): 15839–44. https://doi.org/10.1073/pnas.0506592102.
Newberry, Kate J., et al. “Crystal structure of the Bacillus subtilis anti-alpha, global transcriptional regulator, Spx, in complex with the alpha C-terminal domain of RNA polymerase.Proc Natl Acad Sci U S A, vol. 102, no. 44, Nov. 2005, pp. 15839–44. Pubmed, doi:10.1073/pnas.0506592102.
Newberry KJ, Nakano S, Zuber P, Brennan RG. Crystal structure of the Bacillus subtilis anti-alpha, global transcriptional regulator, Spx, in complex with the alpha C-terminal domain of RNA polymerase. Proc Natl Acad Sci U S A. 2005 Nov 1;102(44):15839–15844.
Journal cover image

Published In

Proc Natl Acad Sci U S A

DOI

ISSN

0027-8424

Publication Date

November 1, 2005

Volume

102

Issue

44

Start / End Page

15839 / 15844

Location

United States

Related Subject Headings

  • Transcription, Genetic
  • Repressor Proteins
  • Protein Structure, Tertiary
  • Protein Binding
  • Oxidation-Reduction
  • Gene Expression Regulation, Bacterial
  • DNA-Directed RNA Polymerases
  • Crystallization
  • Binding Sites
  • Bacterial Proteins