Characterization of the interaction between the saccharomyces cerevisiae Rad51 recombinase and the DNA translocase Rdh54

Sergio R.Santa Maria; Young Ho Kwon; Patrick Sung; Hannah L. Klein

doi:10.1074/jbc.M113.480475

Characterization of the interaction between the saccharomyces cerevisiae Rad51 recombinase and the DNA translocase Rdh54

Sergio R.Santa Maria, Young Ho Kwon, Patrick Sung, Hannah L. Klein

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

11 Scopus citations

Abstract

Background: Rdh54 is a motor protein that is able to dissociate Rad51 recombinase from chromatin. Results: The Rad51-binding domain of Rdh54 resides within its N terminus and is required for Rad51 removal from DNA. Conclusion: Rdh54-Rad51 interaction is important for Rad51 dissociation from chromatin but not for DNA repair. Significance: Rdh54 inhibits accumulation of toxic Rad51-DNA complexes.

Original language	English (US)
Pages (from-to)	21999-22005
Number of pages	7
Journal	Journal of Biological Chemistry
Volume	288
Issue number	30
DOIs	https://doi.org/10.1074/jbc.M113.480475
State	Published - Jul 26 2013
Externally published	Yes

ASJC Scopus subject areas

Molecular Biology
Biochemistry
Cell Biology

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title = "Characterization of the interaction between the saccharomyces cerevisiae Rad51 recombinase and the DNA translocase Rdh54",

abstract = "Background: Rdh54 is a motor protein that is able to dissociate Rad51 recombinase from chromatin. Results: The Rad51-binding domain of Rdh54 resides within its N terminus and is required for Rad51 removal from DNA. Conclusion: Rdh54-Rad51 interaction is important for Rad51 dissociation from chromatin but not for DNA repair. Significance: Rdh54 inhibits accumulation of toxic Rad51-DNA complexes.",

author = "Maria, {Sergio R.Santa} and Kwon, {Young Ho} and Patrick Sung and Klein, {Hannah L.}",

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AU - Maria, Sergio R.Santa

AU - Kwon, Young Ho

AU - Sung, Patrick

AU - Klein, Hannah L.

PY - 2013/7/26

Y1 - 2013/7/26

N2 - Background: Rdh54 is a motor protein that is able to dissociate Rad51 recombinase from chromatin. Results: The Rad51-binding domain of Rdh54 resides within its N terminus and is required for Rad51 removal from DNA. Conclusion: Rdh54-Rad51 interaction is important for Rad51 dissociation from chromatin but not for DNA repair. Significance: Rdh54 inhibits accumulation of toxic Rad51-DNA complexes.

AB - Background: Rdh54 is a motor protein that is able to dissociate Rad51 recombinase from chromatin. Results: The Rad51-binding domain of Rdh54 resides within its N terminus and is required for Rad51 removal from DNA. Conclusion: Rdh54-Rad51 interaction is important for Rad51 dissociation from chromatin but not for DNA repair. Significance: Rdh54 inhibits accumulation of toxic Rad51-DNA complexes.

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Characterization of the interaction between the saccharomyces cerevisiae Rad51 recombinase and the DNA translocase Rdh54

Abstract

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