ArticleMolecular and cellular biology2006
Structure and function of the Saccharomyces cerevisiae Sir3 BAH domain.
Article in Molecular and cellular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 68 citations in OpenAlex.
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- Molecular architecture of nucleosome remodeling and deacetylase sub-complexes by integrative structure determination.Protein science : a publication of the Protein Society · 2022Article
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- The Sir4 H-BRCT domain interacts with phospho-proteins to sequester and repress yeast heterochromatin.The EMBO journal · 2019Article
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- Structure and function of the Orc1 BAH-nucleosome complex.Nature communications · 2019Article
- Adaptive Roles ofG3 (Bethesda, Md.) · 2017Article
- The Nuts and Bolts of Transcriptionally Silent Chromatin in Saccharomyces cerevisiae.Genetics · 2016Review
- Competition between Heterochromatic Loci Allows the Abundance of the Silencing Protein, Sir4, to Regulate de novo Assembly of Heterochromatin.PLoS genetics · 2015Article
- Two Loops Undergoing Concerted Dynamics Regulate the Activity of the ASH1L Histone Methyltransferase.Biochemistry · 2015Article
- Nucleosome structure and function.Chemical reviews · 2015Review
- Solution-state conformation and stoichiometry of yeast Sir3 heterochromatin fibres.Nature communications · 2014Article
- The N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particle.Nature structural & molecular biology · 2013Article
- Nα-acetylated Sir3 stabilizes the conformation of a nucleosome-binding loop in the BAH domain.Nature structural & molecular biology · 2013Article
- The role of the nucleosome acidic patch in modulating higher order chromatin structure.Journal of the Royal Society, Interface · 2013Review
- Sir3 Polymorphisms in Candida glabrata clinical isolates.Mycopathologia · 2013Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Previous work has shown that the N terminus of the Saccharomyces cerevisiae Sir3 protein is crucial for the function of Sir3 in transcriptional silencing. Here, we show that overexpression of N-terminal fragments of Sir3 in strains lacking the full-length protein can lead to some silencing of HML and HMR. Sir3 contains a BAH (bromo-adjacent homology) domain at its N terminus. Overexpression of this domain alone can lead to silencing as long as Sir1 is overexpressed and Sir2 and Sir4 are present. Overexpression of the closely related Orc1 BAH domain can also silence in the absence of any Sir3 protein. A previously characterized hypermorphic sir3 mutation, D205N, greatly improves silencing by the Sir3 BAH domain and allows it to bind to DNA and oligonucleosomes in vitro. A previously uncharacterized region in the Sir1 N terminus is required for silencing by both the Sir3 and Orc1 BAH domains. The structure of the Sir3 BAH domain has been determined. In the crystal, the molecule multimerizes in the form of a left-handed superhelix. This superhelix may be relevant to the function of the BAH domain of Sir3 in silencing.
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Registered trials
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