A Revyakin

AJ Smith

AM Deaconescu

B van den Broek

B Van Houten

C Duboc

CP Selby

DB Srivastava

EEA Verhoeven

EM Witkin

ET Graves

I Mellon

J-S Park

Jun Fan

K Howan

L Manelyte

LF Westblade

Mathieu Leroux-Coyau

MD Wang

Nigel J. Savery

NJ Savery

NM Haines

SC Kou

Terence R. Strick

TR Strick

Y Taniguchi

Crossref

Nature

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

Fan, Jun

Leroux-Coyau, Mathieu

Savery, Nigel J.

Strick, Terence R.

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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.<br/

Savery, Nigel

Strick, Terence R

Explore Bristol Research

English

https://research-information.bris.ac.uk/files/82638015/Reconstruction_of_bacterial_transcription_coupled_repair_at.pdf

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

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Crossref

HAL: Hyper Article en Ligne

Hal-Diderot

HAL Descartes

Explore Bristol Research

Explore Bristol Research