Abstract
The mutL gene of Escherichia coli, which is involved in the repair of mispaired and unpaired nucleotides in DNA, has been independently cloned and the gene product purified. In addition to restoring methyl-directed DNA repair in extracts prepared from mutL strains, the purified MutL protein binds to both double and single stranded DNA. The affinity constant of MutL for unmethylated single stranded DNA was twice that of its affinity constant for methylated single stranded DNA and methylated or unmethylated double stranded DNA. The binding of MutL to double stranded DNA was not affected by the pattern of DNA methylation or the presence of a MutHLS-repairable lesion.
Publication types
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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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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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Chromatography, Gel
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Cloning, Molecular
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Coliphages / genetics
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Coliphages / metabolism
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DNA Repair*
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DNA-Binding Proteins / genetics
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DNA-Binding Proteins / isolation & purification
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DNA-Binding Proteins / metabolism*
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Electrophoresis, Polyacrylamide Gel
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Escherichia coli / genetics
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Escherichia coli / metabolism*
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Genes, Bacterial
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Methylation
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Molecular Sequence Data
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Nucleic Acid Heteroduplexes
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Plasmids
Substances
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Bacterial Proteins
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DNA-Binding Proteins
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Nucleic Acid Heteroduplexes