Human Mus81-Associated Endonuclease Cleaves Holliday Junctions In Vitro

Mus81, a protein with homology to the XPF subunit of the ERCC1-XPF endonuclease, is important for replicational stress tolerance in both budding and fission yeast. Human Mus81 has associated endonuclease activity against structure-specific oligonucleotide substrates, including synthetic Holliday jun...

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Bibliographic Details
Published in:Molecular cell 2001-11, Vol.8 (5), p.1117-1127
Main Authors: Chen, Xiao-Bo, Melchionna, Roberta, Denis, Cecile-Marie, Gaillard, Pierre-Henri L., Blasina, Alessandra, Van de Weyer, Inez, Boddy, Michael N., Russell, Paul, Vialard, Jorge, McGowan, Clare H.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Cell Line
Cloning, Molecular
DNA - metabolism
DNA Damage
DNA Replication - physiology
DNA-Binding Proteins - chemistry
DNA-Binding Proteins - genetics
DNA-Binding Proteins - metabolism
Endonucleases
Fungal Proteins - genetics
Fungal Proteins - metabolism
Humans
Molecular Sequence Data
Mus81 protein
Nuclear Proteins - genetics
Nuclear Proteins - metabolism
Nucleic Acid Conformation
Recombinant Fusion Proteins - metabolism
Saccharomyces cerevisiae Proteins
Sequence Alignment
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Summary:Mus81, a protein with homology to the XPF subunit of the ERCC1-XPF endonuclease, is important for replicational stress tolerance in both budding and fission yeast. Human Mus81 has associated endonuclease activity against structure-specific oligonucleotide substrates, including synthetic Holliday junctions. Mus81-associated endonuclease resolves Holliday junctions into linear duplexes by cutting across the junction exclusively on strands of like polarity. In addition, Mus81 protein abundance increases in cells following exposure to agents that block DNA replication. Taken together, these findings suggest a role for Mus81 in resolving Holliday junctions that arise when DNA replication is blocked by damage or by nucleotide depletion. Mus81 is not related by sequence to previously characterized Holliday junction resolving enzymes, and it has distinct enzymatic properties that suggest it uses a novel enzymatic strategy to cleave Holliday junctions.
ISSN:1097-2765
1097-4164
DOI:10.1016/S1097-2765(01)00375-6