Journal
MOLECULAR CELL
Volume 36, Issue 4, Pages 654-666Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2009.11.009
Keywords
-
Categories
Funding
- MRC [G0501626, MRC G0800970]
- BBSRC [BB/C008316/1, BB/E020690, BB/G005915/1]
- Wellcome Trust [077368/Z/05/Z]
- Biotechnology and Biological Sciences Research Council [BB/C008316/1, BB/G005915/1, BB/E020690/1] Funding Source: researchfish
- Medical Research Council [G0800970, G0501626] Funding Source: researchfish
- BBSRC [BB/E020690/1, BB/G005915/1, BB/C008316/1] Funding Source: UKRI
- MRC [G0501626, G0800970] Funding Source: UKRI
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available