The transcription-repair coupling factor (TRCF, also known as MFD) couples transcription and DNA repair in bacteria. MFD removes transcription elongation complexes stalled at DNA lesions and recruits the nucleotide excision repair (NER) machinery to the site [3]. This protein consists of eight domains [3,4], of which D3 is represented in this entry and its function is unknown. This domain plays a critical role in unmasking of the UvrA binding site [3]. Paper describing PDB structure 2eyq. [1]. 16469698. Structural basis for bacterial transcription-coupled DNA repair. Deaconescu AM, Chambers AL, Smith AJ, Nickels BE, Hochschild A, Savery NJ, Darst SA;. Cell. 2006;124:507-520. Paper describing PDB structure 3hjh. [2]. 19700770. An N-terminal clamp restrains the motor domains of the bacterial transcription-repair coupling factor Mfd. Murphy MN, Gong P, Ralto K, Manelyte L, Savery NJ, Theis K;. Nucleic Acids Res. 2009;37:6042-6053. Paper describing PDB structure 6x26. [3]. 33480355. Structural basis for transcription complex disruption by the Mfd translocase. Kang JY, Llewellyn E, Chen J, Olinares PDB, Brewer J, Chait BT, Campbell EA, Darst SA;. Elife. 2021; [Epub ahead of print]. Paper describing PDB structure 6xeo. [4]. 32719356. Molecular determinants for dsDNA translocation by the transcription-repair coupling and evolvability factor Mfd. Brugger C, Zhang C, Suhanovsky MM, Kim DD, Sinclair AN, Lyumkis D, Deaconescu AM;. Nat Commun. 2020;11:3740. (from Pfam)
- Date:
- 2024-10-16