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• W1976242556 endingPage "13518" @default.
• W1976242556 startingPage "13513" @default.
• W1976242556 abstract "NuA4, the only essential histone acetyltransferase complex in Saccharomyces cerevisiae , acetylates the N-terminal tails of histones H4 and H2A. Affinity purification of NuA4 revealed the presence of three previously undescribed subunits, Vid21/Eaf1/Ydr359c, Swc4/Eaf2/Ygr002c, and Eaf7/Ynl136w. Experimental analyses revealed at least two functionally distinct sets of polypeptides in NuA4: ( i ) Vid21 and Yng2, and ( ii ) Eaf5 and Eaf7. Vid21 and Yng2 are required for bulk histone H4 acetylation and are functionally linked to the histone H2A variant Htz1 and the Swr1 ATPase complex (SWR-C) that assembles Htz1 into chromatin, whereas Eaf5 and Eaf7 have a different, as yet undefined, role. Mutations in Htz1, the SWR-C, and NuA4 cause defects in chromosome segregation that are consistent with genetic interactions we have observed between the genes encoding these proteins and genes encoding kinetochore components. Because SWR-C-dependent recruitment of Htz1 occurs in both transcribed and centromeric regions, a NuA4/SWR-C/Htz1 pathway may regulate both transcription and centromere function in S. cerevisiae ." @default.
• W1976242556 created "2016-06-24" @default.
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• W1976242556 date "2004-09-07" @default.
• W1976242556 modified "2023-10-16" @default.
• W1976242556 title "Regulation of chromosome stability by the histone H2A variant Htz1, the Swr1 chromatin remodeling complex, and the histone acetyltransferase NuA4" @default.
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• W1976242556 doi "https://doi.org/10.1073/pnas.0405753101" @default.
• W1976242556 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/518788" @default.
• W1976242556 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15353583" @default.
• W1976242556 hasPublicationYear "2004" @default.
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