InterPro : IPR004576

Name  Transcription-repair coupling factor Short Name  Mfd
Type  Family Description  The bacterial transcription-repair coupling factor (Mfd) binds to stalled transcription elongation complexes in vitro and catalyses their dissociation from template DNA in an ATP-dependent manner []. A lesion in the template strand blocks the RNA polymerase complex (RNAP). The RNAP-DNA-RNA complex is specifically recognised by Mdf, which releases RNAP and the truncated transcript. Mfd displaces RNAP at the lesion site by pushing the polymerase forward [], allowing the lesion to be accessed by repair proteins []. Mfd contains superfamily II helicase motifs which are essential for the RNAP displacement activity of Mfd [], but does not possess conventional strand-separating helicase activity [].
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

4 Contains

Id Name Short Name Type
IPR001650 Helicase, C-terminal Helicase_C Domain
IPR011545 DEAD/DEAH box helicase domain DEAD/DEAH_box_helicase_dom Domain
IPR003711 CarD-like/TRCF domain CarD-like/TRCF_domain Domain
IPR005118 Transcription-repair-coupling factor, C-terminal domain TRCF_C Domain

0 Found In

0 Parent Features

5 Publications

First Author Title Year Journal Volume Pages
Smith AJ Multipartite control of the DNA translocase, Mfd. 2012 Nucleic Acids Res 40 10408-16
Selby CP Structure and function of transcription-repair coupling factor. II. Catalytic properties. 1995 J Biol Chem 270 4890-5
Manelyte L Regulation and rate enhancement during transcription-coupled DNA repair. 2010 Mol Cell 40 714-24
Park JS E. coli Transcription repair coupling factor (Mfd protein) rescues arrested complexes by promoting forward translocation. 2002 Cell 109 757-67
Roberts J Mfd, the bacterial transcription repair coupling factor: translocation, repair and termination. 2004 Curr Opin Microbiol 7 120-5



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)