Mendillo, Marc L.;
Hargreaves, Victoria V.;
Jamison, Jonathan W.;
Mo, Ashley O.;
Li, Sheng;
Putnam, Christopher D.;
Woods, Virgil L.;
Kolodner, Richard D.
A conserved MutS homolog connector domain interface interacts with MutL homologs
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Medientyp:
E-Artikel
Titel:
A conserved MutS homolog connector domain interface interacts with MutL homologs
Beteiligte:
Mendillo, Marc L.;
Hargreaves, Victoria V.;
Jamison, Jonathan W.;
Mo, Ashley O.;
Li, Sheng;
Putnam, Christopher D.;
Woods, Virgil L.;
Kolodner, Richard D.
Erschienen:
Proceedings of the National Academy of Sciences, 2009
Erschienen in:Proceedings of the National Academy of Sciences
Sprache:
Englisch
DOI:
10.1073/pnas.0912250106
ISSN:
0027-8424;
1091-6490
Entstehung:
Anmerkungen:
Beschreibung:
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<jats:named-content content-type="genus-species">Escherichia coli</jats:named-content>
MutS forms a mispair-dependent ternary complex with MutL that is essential for initiating mismatch repair (MMR) but is structurally uncharacterized, in part owing to its dynamic nature. Here, we used hydrogen/deuterium exchange mass spectrometry and other methods to identify a region in the connector domain (domain II) of MutS that binds MutL and is required for mispair-dependent ternary complex formation and MMR. A structurally conserved region in Msh2, the eukaryotic homolog, was required for formation of a mispair-dependent Msh2–Msh6–Mlh1–Pms1 ternary complex. These data indicate that the connector domain of MutS and Msh2 contains the interface for binding MutL and Mlh1–Pms1, respectively, and support a mechanism whereby mispair and ATP binding induces a conformational change that allows the MutS and Msh2 interfaces to interact with their partners.
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