Abstract
The recombination of DNA molecules has been reconstituted in vitro using two purified enzymes from Escherichia coli. RecA protein catalyses homologous pairing and strand exchange reactions to form intermediate DNA structures that are acted upon by RuvC. The newly identified RuvC protein resolves the intermediates by specific endonucleolytic cleavage to produce recombinant DNA molecules.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Proteins / genetics
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Bacterial Proteins / isolation & purification
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Bacterial Proteins / metabolism*
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Base Sequence
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Binding Sites
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Cloning, Molecular
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DNA, Bacterial / genetics
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Electrophoresis, Polyacrylamide Gel
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Endodeoxyribonucleases*
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Escherichia coli / genetics*
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Escherichia coli / metabolism
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Escherichia coli Proteins*
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Genes, Bacterial
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Macromolecular Substances
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Models, Genetic
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Molecular Sequence Data
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Molecular Weight
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Oligodeoxyribonucleotides
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Plasmids
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Rec A Recombinases / isolation & purification
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Rec A Recombinases / metabolism*
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Recombinant Proteins / isolation & purification
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Recombinant Proteins / metabolism
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Recombination, Genetic*
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Sequence Homology, Nucleic Acid
Substances
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Bacterial Proteins
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DNA, Bacterial
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Escherichia coli Proteins
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Macromolecular Substances
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Oligodeoxyribonucleotides
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Recombinant Proteins
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ruvC protein, E coli
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Rec A Recombinases
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Endodeoxyribonucleases