Chemical trapping of the dynamic MutS-MutL complex formed in DNA mismatch repair in Escherichia coli.

ABSTRACT: The ternary complex comprising MutS, MutL, and DNA is a key intermediate in DNA mismatch repair. We used chemical cross-linking and fluorescence resonance energy transfer (FRET) to study the interaction between MutS and MutL and to shed light onto the structure of this complex. Via chemical cross-linking, we could stabilize this dynamic complex and identify the structural features of key events in DNA mismatch repair. We could show that in the complex between MutS and MutL the mismatch-binding and connector domains of MutS are in proximity to the N-terminal ATPase domain of MutL. The DNA- and nucleotide-dependent complex formation could be monitored by FRET using single cysteine variants labeled in the connector domain of MutS and the transducer domain of MutL, respectively. In addition, w

SUBMITTER: Winkler I 

PROVIDER: S-EPMC3089574 | biostudies-literature | 2011 May

REPOSITORIES: biostudies-literature