Stimulation of Dmc1-mediated DNA strand exchange by the human Rad54B protein

The process of homologous recombination is indispensable for both meiotic and mitotic cell division, and is one of the major pathways for double-strand break (DSB) repair. The human Rad54B protein, which belongs to the SWI2/SNF2 protein family, plays a role in homologous recombination, and may funct...

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Detalles Bibliográficos
Autores principales: Sarai, Naoyuki, Kagawa, Wataru, Kinebuchi, Takashi, Kagawa, Ako, Tanaka, Kozo, Miyagawa, Kiyoshi, Ikawa, Shukuko, Shibata, Takehiko, Kurumizaka, Hitoshi, Yokoyama, Shigeyuki
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2006
Materias:
Molecular Biology
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1636354/
https://www.ncbi.nlm.nih.gov/pubmed/16945962
http://dx.doi.org/10.1093/nar/gkl562
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author Sarai, Naoyuki
Kagawa, Wataru
Kinebuchi, Takashi
Kagawa, Ako
Tanaka, Kozo
Miyagawa, Kiyoshi
Ikawa, Shukuko
Shibata, Takehiko
Kurumizaka, Hitoshi
Yokoyama, Shigeyuki
author_facet Sarai, Naoyuki
Kagawa, Wataru
Kinebuchi, Takashi
Kagawa, Ako
Tanaka, Kozo
Miyagawa, Kiyoshi
Ikawa, Shukuko
Shibata, Takehiko
Kurumizaka, Hitoshi
Yokoyama, Shigeyuki
author_sort Sarai, Naoyuki
collection PubMed
description The process of homologous recombination is indispensable for both meiotic and mitotic cell division, and is one of the major pathways for double-strand break (DSB) repair. The human Rad54B protein, which belongs to the SWI2/SNF2 protein family, plays a role in homologous recombination, and may function with the Dmc1 recombinase, a meiosis-specific Rad51 homolog. In the present study, we found that Rad54B enhanced the DNA strand-exchange activity of Dmc1 by stabilizing the Dmc1–single-stranded DNA (ssDNA) complex. Therefore, Rad54B may stimulate the Dmc1-mediated DNA strand exchange by stabilizing the nucleoprotein filament, which is formed on the ssDNA tails produced at DSB sites during homologous recombination.
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spelling pubmed-16363542006-11-29 Stimulation of Dmc1-mediated DNA strand exchange by the human Rad54B protein Sarai, Naoyuki Kagawa, Wataru Kinebuchi, Takashi Kagawa, Ako Tanaka, Kozo Miyagawa, Kiyoshi Ikawa, Shukuko Shibata, Takehiko Kurumizaka, Hitoshi Yokoyama, Shigeyuki Nucleic Acids Res Molecular Biology The process of homologous recombination is indispensable for both meiotic and mitotic cell division, and is one of the major pathways for double-strand break (DSB) repair. The human Rad54B protein, which belongs to the SWI2/SNF2 protein family, plays a role in homologous recombination, and may function with the Dmc1 recombinase, a meiosis-specific Rad51 homolog. In the present study, we found that Rad54B enhanced the DNA strand-exchange activity of Dmc1 by stabilizing the Dmc1–single-stranded DNA (ssDNA) complex. Therefore, Rad54B may stimulate the Dmc1-mediated DNA strand exchange by stabilizing the nucleoprotein filament, which is formed on the ssDNA tails produced at DSB sites during homologous recombination. Oxford University Press 2006-09 2006-08-31 /pmc/articles/PMC1636354/ /pubmed/16945962 http://dx.doi.org/10.1093/nar/gkl562 Text en © 2006 The Author(s)
spellingShingle Molecular Biology
Sarai, Naoyuki
Kagawa, Wataru
Kinebuchi, Takashi
Kagawa, Ako
Tanaka, Kozo
Miyagawa, Kiyoshi
Ikawa, Shukuko
Shibata, Takehiko
Kurumizaka, Hitoshi
Yokoyama, Shigeyuki
Stimulation of Dmc1-mediated DNA strand exchange by the human Rad54B protein
title Stimulation of Dmc1-mediated DNA strand exchange by the human Rad54B protein
title_full Stimulation of Dmc1-mediated DNA strand exchange by the human Rad54B protein
title_fullStr Stimulation of Dmc1-mediated DNA strand exchange by the human Rad54B protein
title_full_unstemmed Stimulation of Dmc1-mediated DNA strand exchange by the human Rad54B protein
title_short Stimulation of Dmc1-mediated DNA strand exchange by the human Rad54B protein
title_sort stimulation of dmc1-mediated dna strand exchange by the human rad54b protein
topic Molecular Biology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1636354/
https://www.ncbi.nlm.nih.gov/pubmed/16945962
http://dx.doi.org/10.1093/nar/gkl562
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