title: Histone H3 N-terminal acetylation sites especially K14 are important for rDNA silencing and aging.
abstract: Histone variants and histone modifications are essential components in the establishment and maintenance of the repressed status of heterochromatin. Among these histone variants and modifications, acetylation at histone H4K16 is uniquely important for the maintenance of silencing at telomere and mating type loci but not at the ribosomal DNA locus. Here we show that mutations at H3 N-terminal acetylation site K14 specifically disrupt rDNA silencing. However, the mutant ion at H3K14R doesn't affect the recruitment of Pol II repressor RENT (regulator of nucleolar silencing and telophase exit) complex at the rDNA region. Instead, the CAF-1(chromatin assembly factor I) subunit Cac2 level decreased in the H3K14R mutant. Further experiments revealed that the single mutation at H3K14 and multi-site mutations at H3 N-terminus including K14 also delayed replication-depend nucleosome assembly and advanced replicative life span. In conclusion, our data suggest that histone H3 N-terminal acetylation sites especially at K14 are important for rDNA silencing and aging.
authors.affiliation: Jiangsu Key Laboratory of Marine Pharmaceutical Compound Screening, Huaihai Institute of Technology, Lianyungang 222005, China.|Co-Innovation Center of Jiangsu Marine Bio-industry Technology, Lianyungang, 222005, China.
authors.forename: Heng-hao
authors.initials: HH
authors.lastname: Xu
authors.affiliation: Department of Biological Chemistry, David Geffen School of Medicine, University of California, Los Angeles, CA 90095, USA.
authors.forename: Trent
authors.initials: T
authors.lastname: Su
authors.affiliation: Jiangsu Key Laboratory of Marine Pharmaceutical Compound Screening, Huaihai Institute of Technology, Lianyungang 222005, China.|Department of Biological Chemistry, David Geffen School of Medicine, University of California, Los Angeles, CA 90095, USA.
authors.forename: Yong
authors.initials: Y
authors.lastname: Xue
mesh_terms: D000107:Acetylation; D056504:Chromatin Assembly Factor-1 / Q000235:genetics / Q000378:metabolism; D042002:Chromatin Assembly and Disassembly; D047369:Chromatin Immunoprecipitation; D004275:DNA, Ribosomal / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism*; D020868:Gene Silencing; D006657:Histones / Q000235:genetics / Q000378:metabolism*; D016297:Mutagenesis, Site-Directed; D009707:Nucleosomes / Q000378:metabolism; D060888:Real-Time Polymerase Chain Reaction; D012260:Ribonucleases / Q000235:genetics / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism; D013997:Time Factors
chemical_list: C533590:CAC2 protein, S cerevisiae; D056504:Chromatin Assembly Factor-1; D004275:DNA, Ribosomal; D006657:Histones; D009707:Nucleosomes; D029701:Saccharomyces cerevisiae Proteins; D012260:Ribonucleases; C079009:POP2 protein, S cerevisiae