Reconstruction of bacterial transcription-coupled repair at single-molecule resolution

Jun Fan, Mathieu Leroux-Coyau, Nigel Savery, Terence R Strick

Research output: Contribution to journalArticle (Academic Journal)peer-review

47 Citations (Scopus)
481 Downloads (Pure)


Escherichia coli Mfd translocase enables transcription-coupled repair by displacing RNA polymerase (RNAP) stalled on a DNA lesion and then coordinating assembly of the UvrAB(C) components at the damage site1, 2, 3, 4. Recent studies have shown that after binding to and dislodging stalled RNAP, Mfd remains on the DNA in the form of a stable, slowly translocating complex with evicted RNAP attached5, 6. Here we find, using a series of single-molecule assays, that recruitment of UvrA and UvrAB to Mfd–RNAP arrests the translocating complex and causes its dissolution. Correlative single-molecule nanomanipulation and fluorescence measurements show that dissolution of the complex leads to loss of both RNAP and Mfd. Subsequent DNA incision by UvrC is faster than when only UvrAB(C) are available, in part because UvrAB binds 20–200 times more strongly to Mfd–RNAP than to DNA damage. These observations provide a quantitative framework for comparing complementary DNA repair pathways in vivo.

Original languageEnglish
Article number19080
Pages (from-to)234-237
Number of pages20
Early online date3 Aug 2016
Publication statusPublished - 11 Aug 2016

Structured keywords

  • Bristol BioDesign Institute

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