| Autor: |
Grilley, M, Welsh, K M, Su, S S, Modrich, P |
| Zdroj: |
Journal of Biological Chemistry; January 1989, Vol. 264 Issue: 2 p1000-1004, 5p |
| Abstrakt: |
The Escherichia coli mutLgene product has been purified to near homogeneity from an overproducing clone. The mutLlocus 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 Å 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. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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