Abstract
Three Drosophila proteins, ERCC1, MUS312, and MEI-9, function in a complex proposed to resolve double-Holliday-junction intermediates into crossovers during meiosis. We report here the characterization of hold'em (hdm), whose protein product belongs to a single-strand-DNA-binding superfamily of proteins. Mutations in hdm result in reduced meiotic crossover formation and sensitivity to the DNA-damaging agent methyl methanesulfonate. Furthermore, HDM physically interacts with both MEI-9 and ERCC1 in a yeast two-hybrid assay. We conclude that HDM, MEI-9, MUS312, and ERCC1 form a complex that resolves meiotic recombination intermediates into crossovers.
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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Animals
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Chromosome Mapping
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Crossing Over, Genetic* / drug effects
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DNA Breaks, Double-Stranded / drug effects
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DNA Repair* / drug effects
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DNA-Binding Proteins / chemistry
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DNA-Binding Proteins / metabolism*
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Drosophila Proteins / chemistry
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Drosophila Proteins / metabolism*
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Drosophila melanogaster / cytology
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Drosophila melanogaster / drug effects
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Drosophila melanogaster / enzymology*
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Drosophila melanogaster / genetics
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Meiosis*
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Methyl Methanesulfonate / toxicity
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Molecular Sequence Data
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Mutagens / toxicity
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Mutation / genetics
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Nondisjunction, Genetic / drug effects
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Nuclear Proteins / metabolism*
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Protein Binding / drug effects
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Protein Subunits / metabolism
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Two-Hybrid System Techniques
Substances
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DNA-Binding Proteins
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Drosophila Proteins
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ERCC1 protein, Drosophila
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MEI-9 protein, Drosophila
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Mutagens
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Nuclear Proteins
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Protein Subunits
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hdm protein, Drosophila
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Methyl Methanesulfonate