Direct rescue of stalled DNA replication forks via the combined action of PriA and RecG helicase activities

Molecular Cell

Volumn 9, Issue 2, 2002, Pages 241-251

  Gregg, Amanda V ^a   McGlynn, Peter ^a   Jaktaji, Razieh P ^a   Lloyd, Robert G ^a  

^a UNIVERSITY OF NOTTINGHAM   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; HELICASE; M PROTEIN;

ARTICLE; CONTROLLED STUDY; DNA REPLICATION; DNA TEMPLATE; ENZYME ACTIVITY; GENETICS; MODEL; NONHUMAN; PROTEIN STRUCTURE; REGULATORY MECHANISM; SIGNAL TRANSDUCTION; SURVIVAL;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0036184234     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(02)00455-0     Document Type: Article

References (46)

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32. The DNA replication protein PriA and the recombination protein RecG bind D-loops
33. Formation of Holliday junctions by regression of stalled replication forks: RecG stimulates fork regression even when the DNA is negatively supercoiled
34. Resolution of holliday junctions by RuvABC prevents dimer formation in rep mutants and UV-irradiated cells
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38. When checkpoints fail
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43. RuvAB acts at arrested replication forks
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45. Purification and characterization of DnaC810, a primosomal protein capable of bypassing PriA function
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