The transcription-repair coupling factor Mfd associates with RNA polymerase in the absence of exogenous damage

Han N. Ho, Antoine M. Oijen and Harshad Ghodke ()
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Han N. Ho: University of Wollongong, and Illawarra Health and Medical Research Institute
Antoine M. Oijen: University of Wollongong, and Illawarra Health and Medical Research Institute
Harshad Ghodke: University of Wollongong, and Illawarra Health and Medical Research Institute

Nature Communications, 2018, vol. 9, issue 1, 1-12

Abstract: Abstract During transcription elongation, bacterial RNA polymerase (RNAP) can pause, backtrack or stall when transcribing template DNA. Stalled transcription elongation complexes at sites of bulky lesions can be rescued by the transcription terminator Mfd. The molecular mechanisms of Mfd recruitment to transcription complexes in vivo remain to be elucidated, however. Using single-molecule live-cell imaging, we show that Mfd associates with elongation transcription complexes even in the absence of exogenous genotoxic stresses. This interaction requires an intact RNA polymerase-interacting domain of Mfd. In the presence of drugs that stall RNAP, we find that Mfd associates pervasively with RNAP. The residence time of Mfd foci reduces from 30 to 18 s in the presence of endogenous UvrA, suggesting that UvrA promotes the resolution of Mfd-RNAP complexes on DNA. Our results reveal that RNAP is frequently rescued by Mfd during normal growth and highlight a ubiquitous house-keeping role for Mfd in regulating transcription elongation.

Date: 2018
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DOI: 10.1038/s41467-018-03790-z

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