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The crystal structure of the RsbN-σBldN complex from Streptomyces venezuelae defines a new structural class of anti-σ factor.

Publication ,  Journal Article
Schumacher, MA; Bush, MJ; Bibb, MJ; Ramos-León, F; Chandra, G; Zeng, W; Buttner, MJ
Published in: Nucleic Acids Res
August 21, 2018

Streptomyces are filamentous bacteria with a complex developmental life cycle characterized by the formation of spore-forming aerial hyphae. Transcription of the chaplin and rodlin genes, which are essential for aerial hyphae production, is directed by the extracytoplasmic function (ECF) σ factor BldN, which is in turn controlled by an anti-σ factor, RsbN. RsbN shows no sequence similarity to known anti-σ factors and binds and inhibits BldN in an unknown manner. Here we describe the 2.23 Å structure of the RsbN-BldN complex. The structure shows that BldN harbors σ2 and σ4 domains that are individually similar to other ECF σ domains, which bind -10 and -35 promoter regions, respectively. The anti-σ RsbN consists of three helices, with α3 forming a long helix embraced between BldN σ2 and σ4 while RsbN α1-α2 dock against σ4 in a manner that would block -35 DNA binding. RsbN binding also freezes BldN in a conformation inactive for simultaneous -10 and -35 promoter interaction and RNAP binding. Strikingly, RsbN is structurally distinct from previously solved anti-σ proteins. Thus, these data characterize the molecular determinants controlling a central Streptomyces developmental switch and reveal RsbN to be the founding member of a new structural class of anti-σ factor.

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Published In

Nucleic Acids Res

DOI

EISSN

1362-4962

Publication Date

August 21, 2018

Volume

46

Issue

14

Start / End Page

7405 / 7417

Location

England

Related Subject Headings

  • Transcription, Genetic
  • Streptomyces
  • Sigma Factor
  • Sequence Homology, Amino Acid
  • Protein Domains
  • Protein Binding
  • Promoter Regions, Genetic
  • Multiprotein Complexes
  • Models, Molecular
  • Gene Expression Regulation, Bacterial
 

Citation

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Schumacher, M. A., Bush, M. J., Bibb, M. J., Ramos-León, F., Chandra, G., Zeng, W., & Buttner, M. J. (2018). The crystal structure of the RsbN-σBldN complex from Streptomyces venezuelae defines a new structural class of anti-σ factor. Nucleic Acids Res, 46(14), 7405–7417. https://doi.org/10.1093/nar/gky493
Schumacher, Maria A., Matthew J. Bush, Maureen J. Bibb, Félix Ramos-León, Govind Chandra, Wenjie Zeng, and Mark J. Buttner. “The crystal structure of the RsbN-σBldN complex from Streptomyces venezuelae defines a new structural class of anti-σ factor.Nucleic Acids Res 46, no. 14 (August 21, 2018): 7405–17. https://doi.org/10.1093/nar/gky493.
Schumacher MA, Bush MJ, Bibb MJ, Ramos-León F, Chandra G, Zeng W, et al. The crystal structure of the RsbN-σBldN complex from Streptomyces venezuelae defines a new structural class of anti-σ factor. Nucleic Acids Res. 2018 Aug 21;46(14):7405–17.
Schumacher, Maria A., et al. “The crystal structure of the RsbN-σBldN complex from Streptomyces venezuelae defines a new structural class of anti-σ factor.Nucleic Acids Res, vol. 46, no. 14, Aug. 2018, pp. 7405–17. Pubmed, doi:10.1093/nar/gky493.
Schumacher MA, Bush MJ, Bibb MJ, Ramos-León F, Chandra G, Zeng W, Buttner MJ. The crystal structure of the RsbN-σBldN complex from Streptomyces venezuelae defines a new structural class of anti-σ factor. Nucleic Acids Res. 2018 Aug 21;46(14):7405–7417.
Journal cover image

Published In

Nucleic Acids Res

DOI

EISSN

1362-4962

Publication Date

August 21, 2018

Volume

46

Issue

14

Start / End Page

7405 / 7417

Location

England

Related Subject Headings

  • Transcription, Genetic
  • Streptomyces
  • Sigma Factor
  • Sequence Homology, Amino Acid
  • Protein Domains
  • Protein Binding
  • Promoter Regions, Genetic
  • Multiprotein Complexes
  • Models, Molecular
  • Gene Expression Regulation, Bacterial