Structural basis for the role of the Sir3 AAA + domain in silencing: Interaction with Sir4 and unmethylated histone H3K79

Genes and Development

Volumn 25, Issue 17, 2011, Pages 1835-1846

  Ehrentraut, Stefan ^a,d,e   Hassler, Markus ^b,e   Oppikofer, Mariano ^c   Kueng, Stephanie ^c   Weber, Jan M ^a   Mueller, Jonathan W ^a   Gasser, Susan M ^c   Ladurner, Andreas G ^b,e   Ehrenhofer Murray, Ann E ^a  

^a UNIVERSITY OF DUISBURG ESSEN   (Germany)

^b EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^c FRIEDRICH MIESCHER INSTITUTE FOR BIOMEDICAL RESEARCH   (Switzerland)

^d LEIBNIZ INSTITUTE DSMZ GERMAN COLLECTION OF MICROORGANISMS AND CELL CULTURES   (Germany)

^e UNIVERSITY OF MUNICH   (Germany)

Author keywords

Gene silencing; HML; HMR; SIR complex; Sir2; Telomere

Indexed keywords

HISTONE; HISTONE H2K79; SILENT INFORMATION REGULATOR PROTEIN; SILENT INFORMATION REGULATOR PROTEIN 3; SILENT INFORMATION REGULATOR PROTEIN 4; UNCLASSIFIED DRUG;

ARTICLE; GENE SILENCING; HISTONE METHYLATION; IN VITRO STUDY; IN VIVO STUDY; MUTAGENESIS; MUTATION; NONHUMAN; NUCLEOSOME; NUCLEOTIDE BINDING SITE; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; SACCHAROMYCES CEREVISIAE;

ALLELES; CHROMATIN; DNA METHYLATION; GENE SILENCING; HISTONES; MODELS, MOLECULAR; MUTATION; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE; SILENT INFORMATION REGULATOR PROTEINS, SACCHAROMYCES CEREVISIAE;

SACCHAROMYCES CEREVISIAE;

EID: 80052437561     PISSN: 08909369     EISSN: 15495477     Source Type: Journal    
DOI: 10.1101/gad.17175111     Document Type: Article

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