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

Guy, C.P.; Atkinson, J.; Gupta, M.K.; Mahdi, A.A.; Gwynn, E.J.; Rudolph, C.J.; Moon, P.B.; van Knippenberg, I.C.; Cadman, C.J.; Dillingham, M.S.; Lloyd, R.G.; McGlynn, P.


C.P. Guy

J. Atkinson

M.K. Gupta

A.A. Mahdi

E.J. Gwynn

C.J. Rudolph

P.B. Moon

C.J. Cadman

M.S. Dillingham

R.G. Lloyd

P. McGlynn


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.


Guy, C., Atkinson, J., Gupta, M., Mahdi, A., Gwynn, E., Rudolph, C., …McGlynn, P. (2009). Rep provides a second motor at the replisome to promote duplication of protein-bound DNA. Molecular Cell, 36(4), 654-666.

Journal Article Type Article
Publication Date 2009-11
Deposit Date Jul 19, 2023
Journal Molecular cell
Print ISSN 1097-2765
Publisher Elsevier
Peer Reviewed Peer Reviewed
Volume 36
Issue 4
Pages 654-666

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