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

被引:113
作者
Gregg, AV [1 ]
McGlynn, P [1 ]
Jaktaji, RP [1 ]
Lloyd, RG [1 ]
机构
[1] Univ Nottingham, Queens Med Ctr, Inst Genet, Nottingham NG7 2UH, England
基金
英国生物技术与生命科学研究理事会;
关键词
D O I
10.1016/S1097-2765(02)00455-0
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The PriA protein of Escherichia coli plays a key role in the rescue of replication forks stalled on the template DNA. One attractive model of rescue relies on homologous recombination to establish a new fork via PriA-mediated loading of the DnaB replicative helicase at D loop intermediates. We provide genetic and biochemical evidence that PriA helicase activity can also rescue a stalled fork by an alternative mechanism that requires manipulation of the fork before loading of DnaB on the lagging strand template. This direct rescue depends on RecG, which unwinds forks and Holliday junctions and interconverts these structures. The combined action of PriA and RecG helicase activities may thus avoid the potential dangers of rescue pathways Involving fork breakage and recombination.
引用
收藏
页码:241 / 251
页数:11
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