Journal article
Human Rad54 protein stimulates human Mus81–Eme1 endonuclease
Proceedings of the National Academy of Sciences - PNAS, v 105(47), pp 18249-18254
25 Nov 2008
PMID: 19017809
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Rad54, a key protein of homologous recombination, physically interacts with a DNA structure-specific endonuclease, Mus81–Eme1. Genetic data indicate that Mus81–Eme1 and Rad54 might function together in the repair of damaged DNA. In vitro, Rad54 promotes branch migration of Holliday junctions, whereas the Mus81–Eme1 complex resolves DNA junctions by endonucleolytic cleavage. Here, we show that human Rad54 stimulates Mus81–Eme1 endonuclease activity on various Holliday junction-like intermediates. This stimulation is the product of specific interactions between the human Rad54 (hRad54) and Mus81 proteins, considering that
Saccharomyces cerevisiae
Rad54 protein does not stimulate human Mus81–Eme1 endonuclease activity. Stimulation of Mus81–Eme1 cleavage activity depends on formation of specific Rad54 complexes on DNA substrates occurring in the presence of ATP and, to a smaller extent, of other nucleotide cofactors. Thus, our results demonstrate a functional link between the branch migration activity of hRad54 and the structure-specific endonuclease activity of hMus81–Eme1, suggesting that the Rad54 and Mus81–Eme1 proteins may cooperate in the processing of Holliday junction-like intermediates during homologous recombination or DNA repair.
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Details
- Title
- Human Rad54 protein stimulates human Mus81–Eme1 endonuclease
- Creators
- Olga M Mazina - Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, PA 19102-1192Alexander V Mazin - Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, PA 19102-1192
- Publication Details
- Proceedings of the National Academy of Sciences - PNAS, v 105(47), pp 18249-18254
- Publisher
- National Academy of Sciences
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biochemistry and Molecular Biology
- Web of Science ID
- WOS:000261489300040
- Scopus ID
- 2-s2.0-57449090470
- Other Identifier
- 991014877815304721
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- Web of Science research areas
- Biochemistry & Molecular Biology