Isolation and characterization of the Escherichia coli mutL gene product - PubMed (original) (raw)

. 1989 Jan 15;264(2):1000-4.

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• PMID: 2536011

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Isolation and characterization of the Escherichia coli mutL gene product

M Grilley et al. J Biol Chem. 1989.

Free article

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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