Abstract
Ku heterodimer is essential for the repair of DNA double-strand breaks (DSBs) by non-homologous end-joining (NHEJ). Ku recruits XLF, also known as Cernunnos, to DSBs. Here we report domain analyses of Ku-XLF interaction. The heterodimeric domain of Ku was found to be sufficient for the recruitment of XLF to DSBs and for the interaction of Ku with XLF. A small C-terminal deletion of XLF completely abolished recruitment of XLF to DSBs and Ku-XLF interaction. This deletion also led to marked reduction of XLF-XRCC4 interaction although the XRCC4-binding site on the XLF N-terminal domain remained intact. These results demonstrate the significance of Ku-XLF interaction in the molecular assembly of NHEJ factors.
Copyright © 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Antigens, Nuclear / chemistry
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Antigens, Nuclear / genetics
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Antigens, Nuclear / metabolism*
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Binding Sites / genetics
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Blotting, Western
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Cell Line, Tumor
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Cells, Cultured
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DNA Breaks, Double-Stranded*
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DNA Repair
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DNA Repair Enzymes / genetics
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DNA Repair Enzymes / metabolism*
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DNA-Binding Proteins / chemistry
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DNA-Binding Proteins / genetics
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DNA-Binding Proteins / metabolism*
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HEK293 Cells
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Humans
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Ku Autoantigen
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Luminescent Proteins / genetics
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Luminescent Proteins / metabolism
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Mice
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Mice, Knockout
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Microscopy, Fluorescence
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Molecular Sequence Data
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Mutation
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Protein Binding
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Protein Multimerization
Substances
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Antigens, Nuclear
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DNA-Binding Proteins
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Luminescent Proteins
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NHEJ1 protein, human
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XRCC4 protein, human
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Xrcc6 protein, human
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Xrcc6 protein, mouse
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Ku Autoantigen
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DNA Repair Enzymes