The alternating ATPase domains of MutS control DNA mismatch repair.
EMBO J
; 22(3): 746-56, 2003 Feb 03.
Article
em En
| MEDLINE
| ID: mdl-12554674
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.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Bactérias
/
Adenosina Trifosfatases
/
Pareamento Incorreto de Bases
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Proteínas de Escherichia coli
/
Proteínas de Ligação a DNA
/
Escherichia coli
Limite:
Animals
/
Humans
Idioma:
En
Revista:
EMBO J
Ano de publicação:
2003
Tipo de documento:
Article
País de afiliação:
Holanda