PMID:9250691
| Citation |
Allen, DJ, Makhov, A, Grilley, M, Taylor, J, Thresher, R, Modrich, P and Griffith, JD (1997) MutS mediates heteroduplex loop formation by a translocation mechanism. EMBO J. 16:4467-76 |
|---|---|
| Abstract |
Interaction of Escherichia coli MutS and MutL with heteroduplex DNA has been visualized by electron microscopy. In a reaction dependent on ATP hydrolysis, complexes between a MutS dimer and a DNA heteroduplex are converted to protein-stabilized, alpha-shaped loop structures with the mismatch in most cases located within the DNA loop. Loop formation depends on ATP hydrolysis and loop size increases linearly with time at a rate of 370 base pairs/min in phosphate buffer and about 10,000 base pairs/min in the HEPES buffer used for repair assay. These observations suggest a translocation mechanism in which a MutS dimer bound to a mismatch subsequently leaves this site by ATP-dependent tracking or unidimensional movement that is in most cases bidirectional from the mispair. In view of the bidirectional capability of the methyl-directed pathway, this reaction may play a role in determination of heteroduplex orientation. The rate of MutS-mediated DNA loop growth is enhanced by MutL, and when both proteins are present, both are found at the base of alpha-loop structures, and both can remain associated with excision intermediates produced in later stages of the reaction. |
| Links |
PubMed PMC1170073 Online version:10.1093/emboj/16.14.4467 |
| Keywords |
Adenosine Triphosphatases; Adenosine Triphosphate/metabolism; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; DNA Repair; DNA, Viral/genetics; DNA, Viral/metabolism; DNA-Binding Proteins/genetics; DNA-Binding Proteins/metabolism; Deoxyribonucleases, Type II Site-Specific/metabolism; Dimerization; Electrophoresis, Agar Gel; Escherichia coli/chemistry; Escherichia coli/genetics; Escherichia coli Proteins; Kinetics; Microscopy, Electron; MutS DNA Mismatch-Binding Protein; Nucleic Acid Conformation; Nucleic Acid Heteroduplexes/chemistry; Nucleic Acid Heteroduplexes/metabolism; Nucleic Acid Heteroduplexes/ultrastructure; Protein Conformation |
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