Deciphering the mismatch recognition cycle in MutS and MSH2-MSH6 using normal-mode analysis.

ABSTRACT: Postreplication DNA mismatch repair is essential for maintaining the integrity of genomic information in prokaryotes and eukaryotes. The first step in mismatch repair is the recognition of base-base mismatches and insertions/deletions by bacterial MutS or eukaryotic MSH2-MSH6. Crystal structures of both proteins bound to mismatch DNA reveal a similar molecular architecture but provide limited insight into the detailed molecular mechanism of long-range allostery involved in mismatch recognition and repair initiation. This study describes normal-mode calculations of MutS and MSH2-MSH6 with and without DNA. The results reveal similar protein flexibilities and suggest common dynamic and functional characteristics. A strongly correlated motion is present between the lever domain and ATPase doma

SUBMITTER: Mukherjee S 

PROVIDER: S-EPMC3325129 | biostudies-literature | 2009 Mar

REPOSITORIES: biostudies-literature