Journal article
Human Rad54 protein stimulates DNA strand exchange activity of hRad51 protein in the presence of Ca2
The Journal of biological chemistry, v 279(50), pp 52042-52051
10 Dec 2004
PMID: 15466868
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Rad51 and Rad54 proteins play a key role in homologous recombination in eukaryotes. Recently, we reported that Ca2+ is required in vitro for human Rad51 protein to form an active nucleoprotein filament that is important for the search of homologous DNA and for DNA strand exchange, two critical steps of homologous recombination. Here we find that Ca2+ is also required for hRad54 protein to effectively stimulate DNA strand exchange activity of hRad51 protein. This finding identifies Ca2+ as a universal cofactor of DNA strand exchange promoted by mammalian homologous recombination proteins in vitro. We further investigated the hRad54-dependent stimulation of DNA strand exchange. The mechanism of stimulation appeared to include specific interaction of hRad54 protein with the hRad51 nucleoprotein filament. Our results show that hRad54 protein significantly stimulates homology-independent coaggregation of dsDNA with the filament, which represents an essential step of the search for homologous DNA. The results obtained indicate that hRad54 protein serves as a dsDNA gateway for the hRad51-ssDNA filament, promoting binding and an ATP hydrolysis-dependent translocation of dsDNA during the search for homologous sequences.
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Details
- Title
- Human Rad54 protein stimulates DNA strand exchange activity of hRad51 protein in the presence of Ca2
- Creators
- Olga M Mazina - Department of Biochemistry, Drexel University College of Medicine, Philadelphia, Pennsylvania 19102-1192, USAAlexander V Mazin
- Publication Details
- The Journal of biological chemistry, v 279(50), pp 52042-52051
- Publisher
- ASBMB Publications / Elsevier; United States
- Grant note
- CA100839 / NCI NIH HHS
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biochemistry and Molecular Biology
- Web of Science ID
- WOS:000225493400041
- Scopus ID
- 2-s2.0-10644264232
- Other Identifier
- 991014877821104721
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- Web of Science research areas
- Biochemistry & Molecular Biology