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DNA Helicase II and MutL
Previous studies in this lab and others have shown that UvrD (DNA helicase II) and MutL interact (Hall et. al. (1998) EMBO J. 17:1535). In addition, we and others have shown that MutL dramatically stimulates the unwinding activity of UvrD (Yamaguchi et. al. (1998)JBC 273:9197). Both proteins have roles in methyl-directed mismatch repair as well as roles in maintaining genomic stability. We are using biochemical approaches to determine the mechanism by which MutL stimulates UvrD-catalyzed unwinding. In addition, we intend to evaluate, through genetic studies, the importance of the interaction between these proteins. It is likely that the interaction between MutL and UvrD is essential to (i) efficiently load UvrD onto the nicked DNA substrate and (ii) to load UvrD onto the correct DNA strand to insure unwinding and resection of the DNA in the proper direction during mismatch correction. We are using a combination of biochemical, molecular biological and genetic approaches to address these important questions.
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