Characterization of the ATPase activity of RecG and RuvAB proteins on model fork structures reveals insight into stalled DNA replication fork repair

Syafiq Abd Wahab; Meerim Choi; Piero R. Bianco

doi:10.1074/jbc.M113.500223

Characterization of the ATPase activity of RecG and RuvAB proteins on model fork structures reveals insight into stalled DNA replication fork repair

Syafiq Abd Wahab, Meerim Choi, Piero R. Bianco

Research output: Contribution to journal › Article › peer-review

37 Scopus citations

Abstract

Background: DNA replication fork rescue requires the action of DNA helicases to regress the fork. Results: RecG is more active than RuvAB on substrates that mimic nascent stalled forks, whereas RuvAB is active on Holliday junctions. Conclusion: RecG in concert with SSB regresses stalledDNAreplication forks, producingDNAsubstrates to which RuvAB can bind. Significance: RecG, not RuvAB, regresses stalled DNA replication forks.

Original language	English (US)
Pages (from-to)	26397-26409
Number of pages	13
Journal	Journal of Biological Chemistry
Volume	288
Issue number	37
DOIs	https://doi.org/10.1074/jbc.M113.500223
State	Published - Sep 13 2013
Externally published	Yes

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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10.1074/jbc.M113.500223

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abstract = "Background: DNA replication fork rescue requires the action of DNA helicases to regress the fork. Results: RecG is more active than RuvAB on substrates that mimic nascent stalled forks, whereas RuvAB is active on Holliday junctions. Conclusion: RecG in concert with SSB regresses stalledDNAreplication forks, producingDNAsubstrates to which RuvAB can bind. Significance: RecG, not RuvAB, regresses stalled DNA replication forks.",

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AU - Choi, Meerim

AU - Bianco, Piero R.

PY - 2013/9/13

Y1 - 2013/9/13

N2 - Background: DNA replication fork rescue requires the action of DNA helicases to regress the fork. Results: RecG is more active than RuvAB on substrates that mimic nascent stalled forks, whereas RuvAB is active on Holliday junctions. Conclusion: RecG in concert with SSB regresses stalledDNAreplication forks, producingDNAsubstrates to which RuvAB can bind. Significance: RecG, not RuvAB, regresses stalled DNA replication forks.

AB - Background: DNA replication fork rescue requires the action of DNA helicases to regress the fork. Results: RecG is more active than RuvAB on substrates that mimic nascent stalled forks, whereas RuvAB is active on Holliday junctions. Conclusion: RecG in concert with SSB regresses stalledDNAreplication forks, producingDNAsubstrates to which RuvAB can bind. Significance: RecG, not RuvAB, regresses stalled DNA replication forks.

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Characterization of the ATPase activity of RecG and RuvAB proteins on model fork structures reveals insight into stalled DNA replication fork repair

Abstract

ASJC Scopus subject areas

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