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- W1969664012 abstract "Five MutS homologs (MSH), which form three heterodimeric protein complexes, have been identified in eukaryotes. While the human hMSH2-hMSH3 and hMSH2-hMSH6 heterodimers operate primarily in mitotic mismatch repair (MMR), the biochemical function(s) of the meiosis-specific hMSH4-hMSH5 heterodimer is unknown. Here, we demonstrate that purified hMSH4-hMSH5 binds uniquely to Holliday Junctions. Holliday Junctions stimulate the hMSH4-hMSH5 ATP hydrolysis (ATPase) activity, which is controlled by Holliday Junction-provoked ADP→ATP exchange. ATP binding by hMSH4-hMSH5 induces the formation of a hydrolysis-independent sliding clamp that dissociates from the Holliday Junction crossover region, embracing two homologous duplex DNA arms. Fundamental differences between hMSH2-hMSH6 and hMSH4-hMSH5 Holliday Junction recognition are detailed. Our results support the attractive possibility that hMSH4-hMSH5 stabilizes and preserves a meiotic bimolecular double-strand break repair (DSBR) intermediate." @default.
- W1969664012 created "2016-06-24" @default.
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- W1969664012 creator A5088797133 @default.
- W1969664012 date "2004-08-01" @default.
- W1969664012 modified "2023-10-10" @default.
- W1969664012 title "hMSH4-hMSH5 Recognizes Holliday Junctions and Forms a Meiosis-Specific Sliding Clamp that Embraces Homologous Chromosomes" @default.
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- W1969664012 doi "https://doi.org/10.1016/j.molcel.2004.06.040" @default.
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