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TitleMolecular basis for RNA polymerase-dependent transcription complex recycling by the helicase-like motor protein HelD.
Journal, issue, pagesNat Commun, Vol. 11, Issue 1, Page 6420, Year 2020
Publish dateDec 18, 2020
AuthorsTimothy P Newing / Aaron J Oakley / Michael Miller / Catherine J Dawson / Simon H J Brown / James C Bouwer / Gökhan Tolun / Peter J Lewis /
PubMed AbstractIn bacteria, transcription complexes stalled on DNA represent a major source of roadblocks for the DNA replication machinery that must be removed in order to prevent damaging collisions. Gram- ...In bacteria, transcription complexes stalled on DNA represent a major source of roadblocks for the DNA replication machinery that must be removed in order to prevent damaging collisions. Gram-positive bacteria contain a transcription factor HelD that is able to remove and recycle stalled complexes, but it was not known how it performed this function. Here, using single particle cryo-electron microscopy, we have determined the structures of Bacillus subtilis RNA polymerase (RNAP) elongation and HelD complexes, enabling analysis of the conformational changes that occur in RNAP driven by HelD interaction. HelD has a 2-armed structure which penetrates deep into the primary and secondary channels of RNA polymerase. One arm removes nucleic acids from the active site, and the other induces a large conformational change in the primary channel leading to removal and recycling of the stalled polymerase, representing a novel mechanism for recycling transcription complexes in bacteria.
External linksNat Commun / PubMed:33339820 / PubMed Central
MethodsEM (single particle)
Resolution3.36 Å
Structure data

21920

6wvj

EMDB-21920, PDB-6wvj:
Cryo-EM structure of Bacillus subtilis RNA Polymerase elongation complex
Method: EM (single particle) / Resolution: 3.36 Å

21921

6wvk

EMDB-21921, PDB-6wvk:
Cryo-EM structure of Bacillus subtilis RNA Polymerase in complex with HelD
Method: EM (single particle) / Resolution: 3.36 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-MG:
Unknown entry

Source
  • bacillus subtilis (bacteria)
  • escherichia coli bl21(de3) (bacteria)
  • bacillus subtilis (strain 168) (bacteria)
KeywordsTRANSCRIPTION/DNA/RNA / DNA-DEPENDENT RNA POLYMERASE / TRANSCRIPTION / TRANSCRIPTION-DNA-RNA COMPLEX / RNA POLYMERASE / TRANSFERASE-HELD COMPLEX

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