Isolation and characterization of the Escherichia coli mutL gene product.

Journal Article (Journal Article)

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.

Full Text

Duke Authors

Cited Authors

  • Grilley, M; Welsh, KM; Su, SS; Modrich, P

Published Date

  • January 15, 1989

Published In

Volume / Issue

  • 264 / 2

Start / End Page

  • 1000 - 1004

PubMed ID

  • 2536011

International Standard Serial Number (ISSN)

  • 0021-9258


  • eng

Conference Location

  • United States