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TitleStructural basis for activation of Swi2/Snf2 ATPase RapA by RNA polymerase.
Journal, issue, pagesNucleic Acids Res, Vol. 49, Issue 18, Page 10707-10716, Year 2021
Publish dateOct 11, 2021
AuthorsWei Shi / Wei Zhou / Ming Chen / Yang Yang / Yangbo Hu / Bin Liu /
PubMed AbstractRapA is a bacterial RNA polymerase (RNAP)-associated Swi2/Snf2 ATPase that stimulates RNAP recycling. The ATPase activity of RapA is autoinhibited by its N-terminal domain (NTD) but activated with ...RapA is a bacterial RNA polymerase (RNAP)-associated Swi2/Snf2 ATPase that stimulates RNAP recycling. The ATPase activity of RapA is autoinhibited by its N-terminal domain (NTD) but activated with RNAP bound. Here, we report a 3.4-Å cryo-EM structure of Escherichia coli RapA-RNAP elongation complex, in which the ATPase active site of RapA is structurally remodeled. In this process, the NTD of RapA is wedged open by RNAP β' zinc-binding domain (ZBD). In addition, RNAP β flap tip helix (FTH) forms extensive hydrophobic interactions with RapA ATPase core domains. Functional assay demonstrates that removing the ZBD or FTH of RNAP significantly impairs its ability to activate the ATPase activity of RapA. Our results provide the structural basis of RapA ATPase activation by RNAP, through the active site remodeling driven by the ZBD-buttressed large-scale opening of NTD and the direct interactions between FTH and ATPase core domains.
External linksNucleic Acids Res / PubMed:34428297 / PubMed Central
MethodsEM (single particle)
Resolution3.4 Å
Structure data

23716

7m8e

EMDB-23716, PDB-7m8e:
E.coli RNAP-RapA elongation complex
Method: EM (single particle) / Resolution: 3.4 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-MG:
Unknown entry

Source
  • escherichia coli (E. coli)
KeywordsTRANSFERASE/HYDROLASE/DNA/RNA / Swi2/snf2 / RapA / ATPase / RNA polymerase / TRANSFERASE-HYDROLASE-DNA-RNA complex

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