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TitleThe bacterial multidrug resistance regulator BmrR distorts promoter DNA to activate transcription.
Journal, issue, pagesNat Commun, Vol. 11, Issue 1, Page 6284, Year 2020
Publish dateDec 8, 2020
AuthorsChengli Fang / Linyu Li / Yihan Zhao / Xiaoxian Wu / Steven J Philips / Linlin You / Mingkang Zhong / Xiaojin Shi / Thomas V O'Halloran / Qunyi Li / Yu Zhang /
PubMed AbstractThe MerR-family proteins represent a unique family of bacteria transcription factors (TFs), which activate transcription in a manner distinct from canonical ones. Here, we report a cryo-EM structure ...The MerR-family proteins represent a unique family of bacteria transcription factors (TFs), which activate transcription in a manner distinct from canonical ones. Here, we report a cryo-EM structure of a B. subtilis transcription activation complex comprising B. subtilis six-subunit (2αββ'ωε) RNA Polymerase (RNAP) core enzyme, σ, a promoter DNA, and the ligand-bound B. subtilis BmrR, a prototype of MerR-family TFs. The structure reveals that RNAP and BmrR recognize the upstream promoter DNA from opposite faces and induce four significant kinks from the -35 element to the -10 element of the promoter DNA in a cooperative manner, which restores otherwise inactive promoter activity by shortening the length of promoter non-optimal -35/-10 spacer. Our structure supports a DNA-distortion and RNAP-non-contact paradigm of transcriptional activation by MerR TFs.
External linksNat Commun / PubMed:33293519 / PubMed Central
MethodsEM (single particle)
Resolution4.4 Å
Structure data

30390

7ckq

EMDB-30390, PDB-7ckq:
The cryo-EM structure of B. subtilis BmrR transcription activation complex
Method: EM (single particle) / Resolution: 4.4 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ZN:
Unknown entry

ChemComp-P4P:
TETRAPHENYLPHOSPHONIUM

Source
  • Bacillus subtilis subsp. subtilis str. 168 (bacteria)
  • bacillus subtilis (strain 168) (bacteria)
  • synthetic construct (others)
KeywordsTRANSCRIPTION / RNA polymerase / Transcription activation

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