Title | Structural basis for the bacterial transcription-repair coupling factor/RNA polymerase interaction. |
Publication Type | Journal Article |
Year of Publication | 2010 |
Authors | Westblade LF, Campbell EA, Pukhrambam C, Padovan JC, Nickels BE, Lamour V, Darst SA |
Journal | Nucleic Acids Res |
Volume | 38 |
Issue | 22 |
Pagination | 8357-69 |
Date Published | 2010 Dec |
ISSN | 1362-4962 |
Keywords | Amino Acid Sequence, Amino Acid Substitution, Bacterial Proteins, Crystallography, X-Ray, DNA-Directed RNA Polymerases, Models, Molecular, Molecular Sequence Data, Protein Interaction Domains and Motifs, Transcription Factors, Two-Hybrid System Techniques |
Abstract | 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. |
DOI | 10.1093/nar/gkq692 |
Alternate Journal | Nucleic Acids Res |
PubMed ID | 20702425 |
Grant List | GM073829 / GM / NIGMS NIH HHS / United States RR00862 / RR / NCRR NIH HHS / United States RR022220 / RR / NCRR NIH HHS / United States |
Related Faculty:
Lars Westblade, Ph.D.