Structural basis of silencing: Sir3 BAH domain in complex with a nucleosome at 3.0 Å resolution

Gene silencing is essential for regulating cell fate in eukaryotes. Altered chromatin architectures contribute to maintaining the silenced state in a variety of species. The silent information regulator (Sir) proteins regulate mating type in Saccharomyces cerevisiae. One of these proteins, Sir3, int...

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Vydané v:Science (American Association for the Advancement of Science) Ročník 334; číslo 6058; s. 977
Hlavní autori: Armache, Karim-Jean, Garlick, Joseph D, Canzio, Daniele, Narlikar, Geeta J, Kingston, Robert E
Médium: Journal Article
Jazyk:English
Vydavateľské údaje: United States 18.11.2011
Predmet:
Acetylation
Amino Acid Sequence
Binding Sites
Chemical Phenomena
Crystallography, X-Ray
Gene Silencing
Histones - chemistry
Histones - metabolism
Hydrogen Bonding
Methylation
Models, Molecular
Molecular Sequence Data
Mutagenesis
Mutant Proteins - chemistry
Mutant Proteins - metabolism
Nucleosomes - chemistry
Nucleosomes - metabolism
Nucleosomes - ultrastructure
Protein Folding
Protein Interaction Domains and Motifs
Protein Multimerization
Protein Structure, Tertiary
Saccharomyces cerevisiae - chemistry
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - chemistry
Saccharomyces cerevisiae Proteins - metabolism
Silent Information Regulator Proteins, Saccharomyces cerevisiae - chemistry
Silent Information Regulator Proteins, Saccharomyces cerevisiae - genetics
Silent Information Regulator Proteins, Saccharomyces cerevisiae - metabolism
Static Electricity
ISSN:1095-9203, 1095-9203
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Popis
Shrnutí:Gene silencing is essential for regulating cell fate in eukaryotes. Altered chromatin architectures contribute to maintaining the silenced state in a variety of species. The silent information regulator (Sir) proteins regulate mating type in Saccharomyces cerevisiae. One of these proteins, Sir3, interacts directly with the nucleosome to help generate silenced domains. We determined the crystal structure of a complex of the yeast Sir3 BAH (bromo-associated homology) domain and the nucleosome core particle at 3.0 angstrom resolution. We see multiple molecular interactions between the protein surfaces of the nucleosome and the BAH domain that explain numerous genetic mutations. These interactions are accompanied by structural rearrangements in both the nucleosome and the BAH domain. The structure explains how covalent modifications on H4K16 and H3K79 regulate formation of a silencing complex that contains the nucleosome as a central component.
Bibliografia:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:1095-9203
1095-9203
DOI:10.1126/science.1210915