Format

Send to:

Choose Destination
See comment in PubMed Commons below
Mol Cell. 2009 Nov 25;36(4):654-66. doi: 10.1016/j.molcel.2009.11.009.

Rep provides a second motor at the replisome to promote duplication of protein-bound DNA.

Author information

  • 1Institute of Medical Sciences, University of Aberdeen, Foresterhill, UK.

Abstract

Nucleoprotein complexes present challenges to genome stability by acting as potent blocks to replication. One attractive model of how such conflicts are resolved is direct targeting of blocked forks by helicases with the ability to displace the blocking protein-DNA complex. We show that Rep and UvrD each promote movement of E. coli replisomes blocked by nucleoprotein complexes in vitro, that such an activity is required to clear protein blocks (primarily transcription complexes) in vivo, and that a polarity of translocation opposite that of the replicative helicase is critical for this activity. However, these two helicases are not equivalent. Rep but not UvrD interacts physically and functionally with the replicative helicase. In contrast, UvrD likely provides a general means of protein-DNA complex turnover during replication, repair, and recombination. Rep and UvrD therefore provide two contrasting solutions as to how organisms may promote replication of protein-bound DNA.

PMID:
19941825
[PubMed - indexed for MEDLINE]
PMCID:
PMC2807033
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science Icon for PubMed Central
    Loading ...
    Write to the Help Desk