A conserved MutS homolog connector domain interface interacts with MutL homologs
作者： Marc L. Mendillo , Victoria V. Hargreaves , Jonathan W. Jamison , Ashley O. Mo , Sheng Li
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摘要: Escherichia coli MutS forms a mispair-dependent ternary complex with MutL that is essential for initiating mismatch repair (MMR) but structurally uncharacterized, in part owing to its dynamic nature. Here, we used hydrogen/deuterium exchange mass spectrometry and other methods identify region the connector domain (domain II) of binds required formation MMR. A conserved Msh2, eukaryotic homolog, was Msh2–Msh6–Mlh1–Pms1 complex. These data indicate Msh2 contains interface binding Mlh1–Pms1, respectively, support mechanism whereby mispair ATP induces conformational change allows interfaces interact their partners.
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