Isolation and characterization of the Escherichia coli mutL gene product.
The Escherichia coli mutL gene product has been purified to near homogeneity from an overproducing clone. The mutL locus encodes a polypeptide of 70,000 daltons as determined by denaturing gel electrophoresis. The native molecular weight of MutL protein as calculated from the sedimentation coefficient of 5.5 S and Stokes radius of 61 A is 139,000 daltons, indicating that MutL exists as a dimer in solution. In addition to its ability to complement methyl-directed DNA mismatch repair in mutL-deficient cell-free extracts, DNase I protection experiments demonstrate that the purified MutL protein interacts with the MutS-heteroduplex DNA complex in the presence of ATP.
Grilley
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M
Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710.
Welsh
K M
KM
Su
S S
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Modrich
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D001426:Bacterial Proteins / Q000302:isolation & purification*; D002845:Chromatography / Q000379:methods; D002850:Chromatography, Gel / Q000379:methods; D004260:DNA Repair; D017886:Durapatite; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics*; D005796:Genes; D005798:Genes, Bacterial; D006882:Hydroxyapatites; D007202:Indicators and Reagents; D008970:Molecular Weight
D001426:Bacterial Proteins; D006882:Hydroxyapatites; D007202:Indicators and Reagents; D017886:Durapatite