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PDBsum entry 2mc3
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References listed in PDB file
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Key reference
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Title
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A winged helix domain in human mus81 binds DNA and modulates the endonuclease activity of mus81 complexes.
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Authors
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A.J.Fadden,
S.Schalbetter,
M.Bowles,
R.Harris,
J.Lally,
A.M.Carr,
N.Q.Mcdonald.
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Ref.
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Nucleic Acids Res, 2013,
41,
9741-9752.
[DOI no: ]
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PubMed id
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Abstract
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The MUS81-EME1 endonuclease maintains metazoan genomic integrity by cleaving
branched DNA structures that arise during the resolution of recombination
intermediates. In humans, MUS81 also forms a poorly characterized complex with
EME2. Here, we identify and determine the structure of a winged helix (WH)
domain from human MUS81, which binds DNA. WH domain mutations greatly reduce
binding of the isolated domain to DNA and impact on incision activity of
MUS81-EME1/EME2 complexes. Deletion of the WH domain reduces the endonuclease
activity of both MUS81-EME1 and MUS81-EME2 complexes, and incisions made by
MUS81-EME2 are made closer to the junction on substrates containing a downstream
duplex, such as fork structures and nicked Holliday junctions. WH domain
mutation or deletion in Schizosaccharomyces pombe phenocopies the DNA-damage
sensitivity of strains deleted for mus81. Our results indicate an important role
for the WH domain in both yeast and human MUS81 complexes.
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