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TitleStructural basis of the mycobacterial stress-response RNA polymerase auto-inhibition via oligomerization.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 484, Year 2023
Publish dateJan 30, 2023
AuthorsZakia Morichaud / Stefano Trapani / Rishi K Vishwakarma / Laurent Chaloin / Corinne Lionne / Joséphine Lai-Kee-Him / Patrick Bron / Konstantin Brodolin /
PubMed AbstractSelf-assembly of macromolecules into higher-order symmetric structures is fundamental for the regulation of biological processes. Higher-order symmetric structure self-assembly by the gene expression ...Self-assembly of macromolecules into higher-order symmetric structures is fundamental for the regulation of biological processes. Higher-order symmetric structure self-assembly by the gene expression machinery, such as bacterial DNA-dependent RNA polymerase (RNAP), has never been reported before. Here, we show that the stress-response σ factor from the human pathogen, Mycobacterium tuberculosis, induces the RNAP holoenzyme oligomerization into a supramolecular complex composed of eight RNAP units. Cryo-electron microscopy revealed a pseudo-symmetric structure of the RNAP octamer in which RNAP protomers are captured in an auto-inhibited state and display an open-clamp conformation. The structure shows that σ is sequestered by the RNAP flap and clamp domains. The transcriptional activator RbpA prevented octamer formation by promoting the initiation-competent RNAP conformation. Our results reveal that a non-conserved region of σ is an allosteric controller of transcription initiation and demonstrate how basal transcription factors can regulate gene expression by modulating the RNAP holoenzyme assembly and hibernation.
External linksNat Commun / PubMed:36717560 / PubMed Central
MethodsEM (single particle)
Resolution3.86 - 6.75 Å
Structure data

14696

7zf2

EMDB-14696, PDB-7zf2:
Protomeric substructure from an octameric assembly of M. tuberculosis RNA polymerase in complex with sigma-b initiation factor
Method: EM (single particle) / Resolution: 3.86 Å

EMDB-14697: M. tuberculosis RNA polymerase in complex with sigma-b initiation factor: octameric assembly of (alpha)2-beta-beta'-omega-sigB protomers.
Method: EM (single particle) / Resolution: 6.3 Å

EMDB-14974: Cryo-EM structure of Mycobacterium tuberculosis RNA polymerase holoenzyme dimer comprising sigma factor SigB, conformation 2
Method: EM (single particle) / Resolution: 6.75 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-MG:
Unknown entry

Source
  • mycobacterium tuberculosis (bacteria)
  • Mycobacterium tuberculosis H37Rv (bacteria)
KeywordsTRANSCRIPTION / RNA polymerase / self-assembly / octamer / tuberculosis / stress response / hibernation

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