Escherichia coli MutL loads DNA helicase II onto DNA.

摘要: Previous studies have shown that MutL physically interacts with UvrD (DNA helicase II) (Hall, M. C., Jordan, J. R., and Matson, S. W. (1998) EMBO 17, 1535–1541) dramatically stimulates the unwinding reaction catalyzed by in presence absence of other protein components methyl-directed mismatch repair pathway (Yamaguchi, M., Dao, V., Modrich, P. Biol. Chem.273, 9197–9201). The mechanism this stimulation was investigated using DNA binding assays, single-turnover assays involving long duplex substrates. results indicate binds loads onto substrate. interaction between are both important for UvrD-catalyzed unwinding. does not clamp substrate; therefore, processivity is increased MutL. implications these discussed, models presented as well role a master coordinator pathway.