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• W2089731808 abstract "The histone chaperone Asf1 and the checkpoint kinase Rad53 are found in a complex in budding yeast cells in the absence of genotoxic stress. Our data suggest that this complex involves at least three interaction sites. One site involves the H3-binding surface of Asf11 with an as yet undefined surface of Rad53. A second site is formed by the Rad53-FHA1 domain binding to Asf1- T 270 phosphorylated by casein kinase II. The third site involves the C-terminal 21 amino acids of Rad53 bound to the conserved Asf1 N-terminal domain. The structure of this site showed that the Rad53 C-terminus binds Asf1 in a remarkably similar manner to peptides derived from the histone cochaperones HirA and CAF-I. We call this binding motif, ( R / K ) R ( I / A / V ) × ( L / P ), the AIP box for Asf1-Interacting Protein box. Furthermore, C-terminal Rad53- F 820 binds the same pocket of Asf1 as does histone H 4- F 100 . Thus Rad53 competes with histones H3-H4 and cochaperones HirA/CAF-I for binding to Asf1. Rad53 is phosphorylated and activated upon genotoxic stress. The Asf1-Rad53 complex dissociated when cells were treated with hydroxyurea but not methyl-methane-sulfonate, suggesting a regulation of the complex as a function of the stress. We identified a rad53 mutation that destabilized the Asf1-Rad53 complex and increased the viability of rad9 and rad24 mutants in conditions of genotoxic stress, suggesting that complex stability impacts the DNA damage response." @default.
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• W2089731808 date "2012-02-09" @default.
• W2089731808 modified "2023-10-02" @default.
• W2089731808 title "Surprising complexity of the Asf1 histone chaperone-Rad53 kinase interaction" @default.
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• W2089731808 doi "https://doi.org/10.1073/pnas.1106023109" @default.
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