Structural basis for the bacterial transcription-repair coupling factor/RNA polymerase interaction Academic Article uri icon


MeSH Major

  • Bacterial Proteins
  • DNA-Directed RNA Polymerases
  • Transcription Factors


  • The transcription-repair coupling factor (TRCF, the product of the mfd gene) is a widely conserved bacterial protein that mediates transcription-coupled DNA repair. TRCF uses its ATP-dependent DNA translocase activity to remove transcription complexes stalled at sites of DNA damage, and stimulates repair by recruiting components of the nucleotide excision repair pathway to the site. A protein/protein interaction between TRCF and the β-subunit of RNA polymerase (RNAP) is essential for TRCF function. CarD (also called CdnL), an essential regulator of rRNA transcription in Mycobacterium tuberculosis, shares a homologous RNAP interacting domain with TRCF and also interacts with the RNAP β-subunit. We determined the 2.9-Å resolution X-ray crystal structure of the RNAP interacting domain of TRCF complexed with the RNAP-β1 domain, which harbors the TRCF interaction determinants. The structure reveals details of the TRCF/RNAP protein/protein interface, providing a basis for the design and interpretation of experiments probing TRCF, and by homology CarD, function and interactions with the RNAP.

publication date

  • December 2010



  • Academic Article



  • eng

PubMed Central ID

  • PMC3001067

Digital Object Identifier (DOI)

  • 10.1093/nar/gkq692

PubMed ID

  • 20702425

Additional Document Info

start page

  • 8357

end page

  • 69


  • 38


  • 22