Abstract
DNA ligase IV catalyses the final ligation step in the non-homologous end-joining (NHEJ) DNA repair pathway and requires interaction of the ligase with the Xrcc4 'genome-guardian', an essential NHEJ factor. Here we report the 3.9 A crystal structure of the Saccharomyces cerevisiae Xrcc4 ortholog ligase interacting factor 1 (Lif1p) complexed with the C-terminal BRCT domains of DNA ligase IV (Lig4p). The structure reveals a novel mode of protein recognition by a tandem BRCT repeat, and in addition provides a molecular basis for a human LIG4 syndrome clinical condition.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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BRCA1 Protein / chemistry
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Crystallization
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Crystallography, X-Ray
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DNA Damage
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DNA Ligase ATP
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DNA Ligases / chemistry*
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DNA Ligases / genetics
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DNA Repair
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DNA, Fungal / genetics
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DNA-Binding Proteins / chemistry*
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DNA-Binding Proteins / genetics
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Molecular Sequence Data
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Molecular Structure
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Protein Structure, Tertiary
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Saccharomyces cerevisiae / enzymology*
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae Proteins / chemistry*
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Saccharomyces cerevisiae Proteins / genetics
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Sequence Homology, Amino Acid
Substances
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BRCA1 Protein
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DNA, Fungal
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DNA-Binding Proteins
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DNL4 protein, S cerevisiae
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LIF1 protein, S cerevisiae
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LIG4 protein, human
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Saccharomyces cerevisiae Proteins
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DNA Ligases
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DNA Ligase ATP