Mediator function of the human Rad51B-Rad51C complex in Rad51/RPA-catalyzed DNA strand exchange

Stefan Sigurdsson; Stephen Van Komen; Wendy Bussen; David Schild; Joanna S. Albala; Patrick Sung

doi:10.1101/gad.935501

Mediator function of the human Rad51B-Rad51C complex in Rad51/RPA-catalyzed DNA strand exchange

Stefan Sigurdsson, Stephen Van Komen, Wendy Bussen, David Schild, Joanna S. Albala, Patrick Sung

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

197 Scopus citations

Abstract

Five Rad51-like proteins, referred to as Rad51 paralogs, have been described in vertebrates. We show that two of them, Rad51B and Rad51C, are associated in a stable complex. Rad51B-Rad51C complex has ssDNA binding and ssDNA-stimulated ATPase activities. We also examined the functional interaction of Rad51B-Rad51C with Rad51 and RPA. Even though RPA enhances Rad51-catalyzed DNA joint formation via removal of secondary structure in the ssDNA substrate, it can also compete with Rad51 for binding to the substrate, leading to suppressed reaction efficiency. The competition by RPA for substrate binding can be partially alleviated by Rad51B-Rad51C. This recombination mediator function of Rad51B-Rad51C is likely required for the assembly of the Rad51-ssDNA nucleoprotein filament in vivo.

Original language	English (US)
Pages (from-to)	3308-3318
Number of pages	11
Journal	Genes and Development
Volume	15
Issue number	24
DOIs	https://doi.org/10.1101/gad.935501
State	Published - Dec 15 2001

Keywords

DNA double-strand break repair
Tumor suppression

ASJC Scopus subject areas

General Medicine

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title = "Mediator function of the human Rad51B-Rad51C complex in Rad51/RPA-catalyzed DNA strand exchange",

abstract = "Five Rad51-like proteins, referred to as Rad51 paralogs, have been described in vertebrates. We show that two of them, Rad51B and Rad51C, are associated in a stable complex. Rad51B-Rad51C complex has ssDNA binding and ssDNA-stimulated ATPase activities. We also examined the functional interaction of Rad51B-Rad51C with Rad51 and RPA. Even though RPA enhances Rad51-catalyzed DNA joint formation via removal of secondary structure in the ssDNA substrate, it can also compete with Rad51 for binding to the substrate, leading to suppressed reaction efficiency. The competition by RPA for substrate binding can be partially alleviated by Rad51B-Rad51C. This recombination mediator function of Rad51B-Rad51C is likely required for the assembly of the Rad51-ssDNA nucleoprotein filament in vivo.",

keywords = "DNA double-strand break repair, Tumor suppression",

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T1 - Mediator function of the human Rad51B-Rad51C complex in Rad51/RPA-catalyzed DNA strand exchange

AU - Sigurdsson, Stefan

AU - Van Komen, Stephen

AU - Bussen, Wendy

AU - Schild, David

AU - Albala, Joanna S.

AU - Sung, Patrick

PY - 2001/12/15

Y1 - 2001/12/15

N2 - Five Rad51-like proteins, referred to as Rad51 paralogs, have been described in vertebrates. We show that two of them, Rad51B and Rad51C, are associated in a stable complex. Rad51B-Rad51C complex has ssDNA binding and ssDNA-stimulated ATPase activities. We also examined the functional interaction of Rad51B-Rad51C with Rad51 and RPA. Even though RPA enhances Rad51-catalyzed DNA joint formation via removal of secondary structure in the ssDNA substrate, it can also compete with Rad51 for binding to the substrate, leading to suppressed reaction efficiency. The competition by RPA for substrate binding can be partially alleviated by Rad51B-Rad51C. This recombination mediator function of Rad51B-Rad51C is likely required for the assembly of the Rad51-ssDNA nucleoprotein filament in vivo.

AB - Five Rad51-like proteins, referred to as Rad51 paralogs, have been described in vertebrates. We show that two of them, Rad51B and Rad51C, are associated in a stable complex. Rad51B-Rad51C complex has ssDNA binding and ssDNA-stimulated ATPase activities. We also examined the functional interaction of Rad51B-Rad51C with Rad51 and RPA. Even though RPA enhances Rad51-catalyzed DNA joint formation via removal of secondary structure in the ssDNA substrate, it can also compete with Rad51 for binding to the substrate, leading to suppressed reaction efficiency. The competition by RPA for substrate binding can be partially alleviated by Rad51B-Rad51C. This recombination mediator function of Rad51B-Rad51C is likely required for the assembly of the Rad51-ssDNA nucleoprotein filament in vivo.

KW - DNA double-strand break repair

KW - Tumor suppression

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Mediator function of the human Rad51B-Rad51C complex in Rad51/RPA-catalyzed DNA strand exchange

Abstract

Keywords

ASJC Scopus subject areas

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