PMID:2536011
| Citation |
Grilley, M, Welsh, KM, Su, SS and Modrich, P (1989) Isolation and characterization of the Escherichia coli mutL gene product. J. Biol. Chem. 264:1000-4 |
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| Abstract |
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. |
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| Keywords |
Bacterial Proteins/isolation & purification; Chromatography/methods; Chromatography, Gel/methods; DNA Repair; Durapatite; Electrophoresis, Polyacrylamide Gel; Escherichia coli/genetics; Genes; Genes, Bacterial; Hydroxyapatites; Indicators and Reagents; Molecular Weight |
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