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Nap1 stimulates homologous recombination by RAD51 and RAD54 in higher-ordered chromatin containing histone H1.
- Source :
-
Scientific reports [Sci Rep] 2014 May 06; Vol. 4, pp. 4863. Date of Electronic Publication: 2014 May 06. - Publication Year :
- 2014
-
Abstract
- Homologous recombination plays essential roles in mitotic DNA double strand break (DSB) repair and meiotic genetic recombination. In eukaryotes, RAD51 promotes the central homologous-pairing step during homologous recombination, but is not sufficient to overcome the reaction barrier imposed by nucleosomes. RAD54, a member of the ATP-dependent nucleosome remodeling factor family, is required to promote the RAD51-mediated homologous pairing in nucleosomal DNA. In higher eukaryotes, most nucleosomes form higher-ordered chromatin containing the linker histone H1. However, the mechanism by which RAD51/RAD54-mediated homologous pairing occurs in higher-ordered chromatin has not been elucidated. In this study, we found that a histone chaperone, Nap1, accumulates on DSB sites in human cells, and DSB repair is substantially decreased in Nap1-knockdown cells. We determined that Nap1 binds to RAD54, enhances the RAD54-mediated nucleosome remodeling by evicting histone H1, and eventually stimulates the RAD51-mediated homologous pairing in higher-ordered chromatin containing histone H1.
- Subjects :
- Adenosine Triphosphatases metabolism
Cell Line
Chromatin genetics
DNA Helicases genetics
DNA Repair genetics
DNA Repair Enzymes genetics
DNA Repair Enzymes metabolism
DNA-Binding Proteins
Escherichia coli genetics
Escherichia coli metabolism
Histones genetics
Humans
Nuclear Proteins genetics
Nucleosomes genetics
Nucleosomes metabolism
Rad51 Recombinase genetics
tRNA Methyltransferases
Chromatin metabolism
DNA Helicases metabolism
Histones metabolism
Homologous Recombination genetics
Nuclear Proteins metabolism
Proteins metabolism
Rad51 Recombinase metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 2045-2322
- Volume :
- 4
- Database :
- MEDLINE
- Journal :
- Scientific reports
- Publication Type :
- Academic Journal
- Accession number :
- 24798879
- Full Text :
- https://doi.org/10.1038/srep04863