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A more recent version of this article appeared on February 1, 2004
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Submitted on August 11, 2003
Revised on October 15, 2003
Accepted on October 15, 2003
1 Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, USA
2 Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, USA, Department of Medicine, University of
California at San Francisco, San Francisco, California 94143
3 Department of Cell Biology, The Scripps Research Institute, La Jolla, California 92037, USA
* Corresponding author. E-mail address: chmcg{at}scripps.edu.
Mus81 is a highly conserved endonuclease with homology to the XPF subunit of the XPF-ERCC1 complex. In yeast Mus81 associates with a second subunit, Eme1 or Mms4, which is essential for endonuclease activity in vitro and for in vivo function. Human Mus81 binds to a homologue of fission yeast Eme1 in vitro and in vivo. We show that recombinant Mus81-Eme1 cleaves replication forks, 3' flap substrates and Holliday junctions in vitro. By use of differentially tagged versions of Mus81 and Eme1 we find that Mus81 associates with Mus81, and that Eme1 associates with Eme1. Thus, complexes containing two or more Mus81-Eme1 U could function to coordinate substrate cleavage in vivo. Down-regulation of Mus81 by RNA interference reduces mitotic recombination in human somatic cells. The recombination defect is rescued by expression of a bacterial Holliday junction resolvase. These data provide direct evidence for a role of Mus81-Eme1 in mitotic recombination in higher eukaryotes and support the hypothesis that Mus81-Eme1 resolves Holliday junctions in vivo.
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