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Stopped in its tracks: the RNA polymerase molecular motor as a robust sensor of DNA damage.

Abstract：

:DNA repair is often a complex, multi-component, multi-step process; this makes detailed kinetic analysis of the different steps of repair a challenging task using standard biochemical methods. At the same time, single-molecule methods are well-suited for extracting kinetic information despite time-averaging due to diffusion of biochemical components and stochasticity of chemical reaction steps. Here we discuss recent experiments using DNA nanomanipulation in a magnetic trap to study the initiation of transcription-coupled repair in a model bacterial system comprising the canonical Escherichia coli RNA polymerase and the Mfd translocase which specifically binds to it. These experiments provide kinetic insight into the reaction process, helping to explain how Mfd discriminates between transcribing RNAP and stalled RNAP. They also identify a reliably long-lived intermediate containing Mfd translocase and, potentially, RNA polymerase. This intermediate presumably serves as a platform for assembly of downstream repair components UvrAB(C).

journal_name

DNA Repair (Amst)

journal_title

DNA repair

authors

Howan K,Monnet J,Fan J,Strick TR

doi

10.1016/j.dnarep.2014.02.018

subject

Has Abstract

pub_date

2014-08-01 00:00:00

pages

49-57

eissn

1568-7864

issn

1568-7856

pii

S1568-7864(14)00059-7

journal_volume

20

pub_type

杂志文章,评审

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