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• W2396216906 abstract "Chromatin Assembly Complex 1 (CAF-1) is a major histone chaperone involved in deposition of histone H3 and H4 into nucleosome. CAF-1 is composed of three subunits; p150, p60 and p48 for human and Cac1, Cac2 and Cac3 for yeast. Despite of its central role in chromatin formation, structural features of the full CAF-1 in complex with histones and other chaperones have not been well characterized. Here, we dissect molecular architecture of yeast CAF-1 (yCAF-1) by cross-linking mass spectrometry (XL-MS) and negative stain single-particle electron microscopy (EM). Our work revealed that Cac1, the largest subunit of yCAF-1, might serve as a major histone binding platform linking Cac2 and Cac3. In addition, EM analysis showed that yCAF-1 adopts a bilobal shape and Cac1 connecting Cac2 and Cac3 to generate a platform for binding histones. This study provides the first structural glimpse of the full CAF-1 complex and a structural framework to understand histone chaperoning processes." @default.
• W2396216906 created "2016-06-24" @default.
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• W2396216906 date "2016-05-25" @default.
• W2396216906 modified "2023-10-09" @default.
• W2396216906 title "Molecular Architecture of Yeast Chromatin Assembly Factor 1" @default.
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• W2396216906 doi "https://doi.org/10.1038/srep26702" @default.
• W2396216906 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4879628" @default.
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