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

Colin P Guy, John Atkinson, Milind K Gupta, Akeel A Mahdi, Emma J Gwynn, Christian J Rudolph, Peter B Moon, Ingeborg C van Knippenberg, Chris J Cadman, Mark S Dillingham, Robert G Lloyd, Peter McGlynn

Research output: Contribution to journalArticlepeer-review

129 Citations (Scopus)


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.
Original languageEnglish
Pages (from-to)654-666
Number of pages13
JournalMolecular Cell
Issue number4
Publication statusPublished - 25 Nov 2009

Bibliographical note

A paid open access option is available for this journal.
Publisher's version/PDF cannot be used


  • culture media
  • DNA helicases
  • DNA replication
  • DNA, bacterial
  • DNA-directed DNA polymerase
  • DnaB helicases
  • Escherichia coli
  • Escherichia coli proteins
  • genetic complementation test
  • molecular motor proteins
  • multienzyme complexes
  • mutation
  • nucleoproteins
  • protein binding
  • suppression, genetic
  • transcription, genetic


Dive into the research topics of 'Rep provides a second motor at the replisome to promote duplication of protein-bound DNA'. Together they form a unique fingerprint.

Cite this