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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 757-767 |
| Number of pages | 11 |
| Journal | Cell |
| Volume | 109 |
| Issue number | 6 |
| DOIs | |
| State | Published - Jun 14 2002 |
Funding
We thank C. Selby and A. Sancar for pMFD19; P. Modrich for Gln111 protein; S. Darst for providing coordinates of the T. aquaticus RNAP elongation complex; Max Gottesman and John Lis for criticizing the manuscript; and Tom Santangelo and Chris Roberts for assistance and help with the manuscript. Supported by grant GM 21941 from the National Institutes of Health.
ASJC Scopus subject areas
- General Biochemistry, Genetics and Molecular Biology