Inhibition of Msh6 ATPase activity by mispaired DNA induces a Msh2(ATP)-Msh6(ATP) state capable of hydrolysis-independent movement along DNA.
Mol Cell
; 22(1): 39-49, 2006 Apr 07.
Article
en En
| MEDLINE
| ID: mdl-16600868
ABSTRACT
The Msh2-Msh6 heterodimer plays a key role in the repair of mispaired bases in DNA. Critical to its role in mismatch repair is the ATPase activity that resides within each subunit. Here we show that both subunits can simultaneously bind ATP and identify the Msh6 subunit as containing the high-affinity ATP binding site and Msh2 as containing a high-affinity ADP binding site. Stable binding of ATP to Msh6 causes decreased affinity of Msh2 for ADP, and binding to mispaired DNA stabilized the binding of ATP to Msh6. Our results support a model in which mispair binding encourages a dual-occupancy state with ATP bound to Msh6 and Msh2; this state supports hydrolysis-independent sliding along DNA.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
ADN
/
Adenosina Trifosfato
/
Adenosina Trifosfatasas
/
Proteínas de Saccharomyces cerevisiae
/
Proteínas de Unión al ADN
/
Proteína 2 Homóloga a MutS
Idioma:
En
Revista:
Mol Cell
Asunto de la revista:
BIOLOGIA MOLECULAR
Año:
2006
Tipo del documento:
Article
País de afiliación:
Estados Unidos