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Isolation and Characterization of the Escherichia coli mutL Gene Product

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Grilley, M, Welsh, K M, Su, S S, Modrich, P·1989·Journal of Biological Chemistry

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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Metadata

Authors
Grilley, M., Welsh, K. M., Su, S. S., & Modrich, P.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1989-01
Volume
264
Issue
2
Pages
1000-1004
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1577360400
Cited by
301
References
0
FWCI
2.73
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Isolation and Characterization of the Escherichia coli mutL Gene Product. https://app.cochat.ai/papers/10.1016/s0021-9258(19)85043-3
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Grilley, M., Welsh, K. M., Su, S. S., & Modrich, P. (1989). Isolation and Characterization of the Escherichia coli mutL Gene Product. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)85043-3

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