The Mfd protein is the transcription-repair coupling factor (TRCF) in Mycobacterium smegmatis

J Biol Chem. 2023 Mar;299(3):103009. doi: 10.1016/j.jbc.2023.103009. Epub 2023 Feb 11.

Abstract

In vitro and in vivo experiments with Escherichia coli have shown that the Mfd translocase is responsible for transcription-coupled repair, a subpathway of nucleotide excision repair involving the faster rate of repair of the transcribed strand than the nontranscribed strand. Even though the mfd gene is conserved in all bacterial lineages, there is only limited information on whether it performs the same function in other bacterial species. Here, by genome scale analysis of repair of UV-induced cyclobutane pyrimidine dimers, we find that the Mfd protein is the transcription-repair coupling factor in Mycobacterium smegmatis. This finding, combined with the inverted strandedness of UV-induced mutations in WT and mfd-E. coli and Bacillus subtilis indicate that the Mfd protein is the universal transcription-repair coupling factor in bacteria.

Keywords: UvrD; excision repair-sequencing; nucleotide excision repair; transcription-coupled repair; tuberculosis.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, N.I.H., Extramural

MeSH terms

  • Bacteria / metabolism
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • DNA Repair
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Mycobacterium smegmatis / genetics
  • Mycobacterium smegmatis / metabolism
  • Transcription Factors* / genetics
  • Transcription Factors* / metabolism
  • Transcription, Genetic*

Substances

  • Transcription Factors
  • Bacterial Proteins