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Isolation and Characterization of the Escherichia coli mutL Gene Product
Open accessAbstract
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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Cited by
Redundancy of Saccharomyces cerevisiae MSH3 and MSH6 in MSH2-dependent mismatch repair
Marsischky, G. T., Filosi, N., Kane, M. F., & Kolodner, R. (1996) · Genes & Development · doi:10.1101/gad.10.4.407 · Cited by 581
Billmyre, R. B., Clancey, S. A., & Heitman, J. (2017) · eLife · doi:10.7554/elife.28802 · Cited by 79
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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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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