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E. coli Transcription repair coupling factor (Mfd protein) rescues arrested complexes by promoting forward translocation.

Authors
Type
Published Article
Journal
Cell
0092-8674
Publisher
Elsevier
Publication Date
Volume
109
Issue
6
Pages
757–767
Identifiers
PMID: 12086674
Source
Medline
License
Unknown

Abstract

Transcription and DNA repair are coupled in E. coli by the Mfd protein, which dissociates transcription elongation complexes blocked at nonpairing lesions and mediates recruitment of DNA repair proteins. We show that Mfd influences the elongation state of RNA polymerase (RNAP); transcription complexes that have reverse translocated into the backtracked position, a potentially important intermediate in RNA proofreading and repair, are restored to the forward position by the activity of Mfd, and arrested complexes are rescued into productive elongation. Mfd may act through a translocase activity that rewinds upstream DNA, leading either to translocation or to release of RNA polymerase when the enzyme active site cannot continue elongation.

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