PMID:12554674
| Citation |
Lamers, MH, Winterwerp, HH and Sixma, TK (2003) The alternating ATPase domains of MutS control DNA mismatch repair. EMBO J. 22:746-56 |
|---|---|
| Abstract |
DNA mismatch repair is an essential safeguard of genomic integrity by removing base mispairings that may arise from DNA polymerase errors or from homologous recombination between DNA strands. In Escherichia coli, the MutS enzyme recognizes mismatches and initiates repair. MutS has an intrinsic ATPase activity crucial for its function, but which is poorly understood. We show here that within the MutS homodimer, the two chemically identical ATPase sites have different affinities for ADP, and the two sites alternate in ATP hydrolysis. A single residue, Arg697, located at the interface of the two ATPase domains, controls the asymmetry. When mutated, the asymmetry is lost and mismatch repair in vivo is impaired. We propose that asymmetry of the ATPase domains is an essential feature of mismatch repair that controls the timing of the different steps in the repair cascade. |
| Links |
PubMed PMC140748 Online version:10.1093/emboj/cdg064 |
| Keywords |
Adenosine Triphosphatases/chemistry; Adenosine Triphosphatases/genetics; Adenosine Triphosphatases/metabolism; Adenosine Triphosphate/metabolism; Adenylyl Imidodiphosphate/metabolism; Amino Acid Sequence; Animals; Bacterial Proteins; Base Pair Mismatch; Crystallography, X-Ray; DNA Repair; DNA-Binding Proteins; Dimerization; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Humans; Models, Molecular; Molecular Sequence Data; MutS DNA Mismatch-Binding Protein; Nucleotides/metabolism; Phenotype; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Sequence Alignment; Vanadates/metabolism |
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