ArticleMolecular and cellular biology2008
Sir3-nucleosome interactions in spreading of silent chromatin in Saccharomyces cerevisiae.
Article in Molecular and cellular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 69 citations in OpenAlex.
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- SUMO is a pervasive regulator of meiosis.eLife · 2021Article
- Structure and function of the Orc1 BAH-nucleosome complex.Nature communications · 2019Article
- Modulation of Gene Silencing by Cdc7p via H4 K16 Acetylation and Phosphorylation of Chromatin Assembly Factor CAF-1 inGenetics · 2019Article
- Discovery and Evolution of New Domains in Yeast Heterochromatin Factor Sir4 and Its Partner Esc1.Genome biology and evolution · 2019Article
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- The Nuts and Bolts of Transcriptionally Silent Chromatin in Saccharomyces cerevisiae.Genetics · 2016Review
- Hypothesis: Paralog Formation from Progenitor Proteins and Paralog Mutagenesis Spur the Rapid Evolution of Telomere Binding Proteins.Frontiers in genetics · 2016Article
- 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
- Heterochromatin protein Sir3 induces contacts between the amino terminus of histone H4 and nucleosomal DNA.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- The role of the nucleosome acidic patch in modulating higher order chromatin structure.Journal of the Royal Society, Interface · 2013Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Silent chromatin in Saccharomyces cerevisiae is established in a stepwise process involving the SIR complex, comprised of the histone deacetylase Sir2 and the structural components Sir3 and Sir4. The Sir3 protein, which is the primary histone-binding component of the SIR complex, forms oligomers in vitro and has been proposed to mediate the spreading of the SIR complex along the chromatin fiber. In order to analyze the role of Sir3 in the spreading of the SIR complex, we performed a targeted genetic screen for alleles of SIR3 that dominantly disrupt silencing. Most mutations mapped to a single surface in the conserved N-terminal BAH domain, while one, L738P, localized to the AAA ATPase-like domain within the C-terminal half of Sir3. The BAH point mutants, but not the L738P mutant, disrupted the interaction between Sir3 and nucleosomes. In contrast, Sir3-L738P bound the N-terminal tail of histone H4 more strongly than wild-type Sir3, indicating that misregulation of the Sir3 C-terminal histone-binding activity also disrupted spreading. Our results underscore the importance of proper interactions between Sir3 and the nucleosome in silent chromatin assembly. We propose a model for the spreading of the SIR complex along the chromatin fiber through the two distinct histone-binding domains in Sir3.
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