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TitleStructural basis of Mfd-dependent transcription termination.
Journal, issue, pagesNucleic Acids Res, Vol. 48, Issue 20, Page 11762-11772, Year 2020
Publish dateNov 18, 2020
AuthorsJing Shi / Aijia Wen / Minxing Zhao / Sha Jin / Linlin You / Yue Shi / Shuling Dong / Xiaoting Hua / Yu Zhang / Yu Feng /
PubMed AbstractMfd-dependent transcription termination plays an important role in transcription-coupled DNA repair, transcription-replication conflict resolution, and antimicrobial resistance development. Despite ...Mfd-dependent transcription termination plays an important role in transcription-coupled DNA repair, transcription-replication conflict resolution, and antimicrobial resistance development. Despite extensive studies, the molecular mechanism of Mfd-dependent transcription termination in bacteria remains unclear, with several long-standing puzzles. How Mfd is activated by stalled RNA polymerase (RNAP) and how activated Mfd translocates along the DNA are unknown. Here, we report the single-particle cryo-electron microscopy structures of T. thermophilus Mfd-RNAP complex with and without ATPγS. The structures reveal that Mfd undergoes profound conformational changes upon activation, contacts the RNAP β1 domain and its clamp, and pries open the RNAP clamp. These structures provide a foundation for future studies aimed at dissecting the precise mechanism of Mfd-dependent transcription termination and pave the way for rational drug design targeting Mfd for the purpose of tackling the antimicrobial resistance crisis.
External linksNucleic Acids Res / PubMed:33068413 / PubMed Central
MethodsEM (single particle)
Resolution3.1 - 5.0 Å
Structure data

30117

6m6a

EMDB-30117: CryoEM structure of Thermus thermophilus transcription-repair coupling complex in the absence of ATP-gamma-S
PDB-6m6a: Cryo-EM structure of Thermus thermophilus Mfd in complex with RNA polymerase
Method: EM (single particle) / Resolution: 5.0 Å

30118

6m6b

EMDB-30118: CryoEM structure of Thermus thermophilus transcription-repair coupling complex in the presence of ATP-gamma-S
PDB-6m6b: Cryo-EM structure of Thermus thermophilus Mfd in complex with RNA polymerase and ATP-gamma-S
Method: EM (single particle) / Resolution: 4.1 Å

30119

6m6c

EMDB-30119, PDB-6m6c:
CryoEM structure of Thermus thermophilus RNA polymerase elongation complex
Method: EM (single particle) / Resolution: 3.1 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-MG:
Unknown entry

ChemComp-AGS:
PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / ATP-gamma-S, energy-carrying molecule analogue*YM

Source
  • thermus thermophilus (bacteria)
  • thermus thermophilus (strain hb8 / atcc 27634 / dsm 579) (bacteria)
  • thermus thermophilus (strain hb27 / atcc baa-163 / dsm 7039) (bacteria)
KeywordsTRANSCRIPTION / RNA polymerase / DNA repair / Mfd

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