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• W2989776593 endingPage "904" @default.
• W2989776593 startingPage "899" @default.
• W2989776593 abstract "DNA clamp, a highly conserved ring-shaped protein, binds dsDNA within its central pore. Also, DNA clamp interacts with various nuclear proteins on its front, thereby stimulating their enzymatic activities and biological functions. It has been assumed that the DNA clamp is a functionally single-faced ring from bacteria to humans. Here, we report the crystal structure of the heterotrimeric RAD9-RAD1-HUS1 (9-1-1) checkpoint clamp bound to a peptide of RHINO, a recently identified cancer-related protein that interacts with 9-1-1 and promotes activation of the DNA damage checkpoint. This is the first structure of 9-1-1 bound to its partner. The structure reveals that RHINO is unexpectedly bound to the edge and around the back of the 9-1-1 ring through specific interactions with the RAD1 subunit of 9-1-1. Our finding indicates that 9-1-1 is a functionally double-faced DNA clamp." @default.
• W2989776593 created "2019-12-05" @default.
• W2989776593 creator A5004155993 @default.
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• W2989776593 date "2019-11-27" @default.
• W2989776593 modified "2023-10-16" @default.
• W2989776593 title "Structure of the RAD9-RAD1-HUS1 checkpoint clamp bound to RHINO sheds light on the other side of the DNA clamp" @default.
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• W2989776593 doi "https://doi.org/10.1074/jbc.ac119.011816" @default.
• W2989776593 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6983850" @default.
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• W2989776593 hasPublicationYear "2019" @default.
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