Abstract
Condensin I is important for chromosome organization and segregation in mitosis. We previously showed that condensin I also interacts with PARP1 in response to DNA damage and plays a role in single-strand break repair. However, whether condensin I physically associates with DNA damage sites and how PARP1 may contribute to this process were unclear. We found that condensin I is preferentially recruited to DNA damage sites enriched for base damage. This process is dictated by PARP1 through its interaction with the chromosome-targeting domain of the hCAP-D2 subunit of condensin I.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Adenosine Triphosphatases / genetics
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Adenosine Triphosphatases / metabolism
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Animals
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Binding Sites / genetics
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Blotting, Western
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Cell Cycle Proteins / genetics
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Cell Cycle Proteins / metabolism*
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Cells, Cultured
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Chromatin Immunoprecipitation
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Chromosomal Proteins, Non-Histone / genetics
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Chromosomal Proteins, Non-Histone / metabolism
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DNA Breaks, Single-Stranded
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DNA Damage*
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DNA Repair*
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DNA-Binding Proteins / genetics
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DNA-Binding Proteins / metabolism
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Embryo, Mammalian / cytology
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Embryo, Mammalian / metabolism
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Fibroblasts / metabolism
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Green Fluorescent Proteins / genetics
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Green Fluorescent Proteins / metabolism
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HeLa Cells
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Humans
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Mice
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Mice, Knockout
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Multiprotein Complexes / genetics
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Multiprotein Complexes / metabolism
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Mutation
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Nuclear Proteins / genetics
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Nuclear Proteins / metabolism*
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Poly (ADP-Ribose) Polymerase-1
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Poly(ADP-ribose) Polymerases / genetics
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Poly(ADP-ribose) Polymerases / metabolism*
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Poly-ADP-Ribose Binding Proteins
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Protein Binding
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RNA Interference
Substances
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Cell Cycle Proteins
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Chromosomal Proteins, Non-Histone
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DNA-Binding Proteins
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Multiprotein Complexes
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NCAPD2 protein, human
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Nuclear Proteins
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Poly-ADP-Ribose Binding Proteins
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condensin complexes
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Green Fluorescent Proteins
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PARP1 protein, human
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Poly (ADP-Ribose) Polymerase-1
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Poly(ADP-ribose) Polymerases
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Adenosine Triphosphatases