ArticleMolecular and cellular biology2009
Mutational analysis of the Sir3 BAH domain reveals multiple points of interaction with nucleosomes.
Article in Molecular and cellular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 50 citations in OpenAlex.
- Unwrap RAP1's Mystery at Kinetoplastid Telomeres.Biomolecules · 2024Review
- Regulation of telomere silencing by the core histones-autophagy-Sir2 axis.Life science alliance · 2023Article
- Article
- Distinct structural groups of histone H3 and H4 residues have divergent effects on chronological lifespan in Saccharomyces cerevisiae.PloS one · 2022Article
- Sir3 mediates long-range chromosome interactions in budding yeast.Genome research · 2021Article
- Variants of the Sir4 Coiled-Coil Domain Improve Binding to Sir3 for Heterochromatin Formation inG3 (Bethesda, Md.) · 2017Article
- The Nuts and Bolts of Transcriptionally Silent Chromatin in Saccharomyces cerevisiae.Genetics · 2016Review
- Review
- Chromatin-dependent repression of the Arabidopsis floral integrator genes involves plant specific PHD-containing proteins.The Plant cell · 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
- 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
- Sir3 Polymorphisms in Candida glabrata clinical isolates.Mycopathologia · 2013Article
- Dimerization of Sir3 via its C-terminal winged helix domain is essential for yeast heterochromatin formation.The EMBO journal · 2013Article
- Changes in the genome-wide localization pattern of Sir3 in Saccharomyces cerevisiae during different growth stages.Computational and structural biotechnology journal · 2013Article
- The role of multiple marks in epigenetic silencing and the emergence of a stable bivalent chromatin state.PLoS computational biology · 2013Article
- Ascending the nucleosome face: recognition and function of structured domains in the histone H2A-H2B dimer.Biochimica et biophysica acta · 2012Article
- The BAH domain of ORC1 links H4K20me2 to DNA replication licensing and Meier-Gorlin syndrome.Nature · 2012Article
- Functions of protosilencers in the formation and maintenance of heterochromatin in Saccharomyces cerevisiae.PloS one · 2012Article
- Structural basis of silencing: Sir3 BAH domain in complex with a nucleosome at 3.0 Å resolution.Science (New York, N.Y.) · 2011Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Sir3, a component of the transcriptional silencing complex in the yeast Saccharomyces cerevisiae, has an N-terminal BAH domain that is crucial for the protein's silencing function. Previous work has shown that the N-terminal alanine residue of Sir3 (Ala2) and its acetylation play an important role in silencing. Here we show that the silencing defects of Sir3 Ala2 mutants can be suppressed by mutations in histones H3 and H4, specifically, by H3 D77N and H4 H75Y mutations. Additionally, a mutational analysis demonstrates that three separate regions of the Sir3 BAH domain are important for its role in silencing. Many of these BAH mutations also can be suppressed by the H3 D77N and H4 H75Y mutations. In agreement with the results of others, in vitro experiments show that the Sir3 BAH domain can interact with partially purified nucleosomes. The silencing-defective BAH mutants are defective for this interaction. These results, together with the previously characterized interaction between the C-terminal region of Sir3 and the histone H3/H4 tails, suggest that Sir3 utilizes multiple domains to interact with nucleosomes.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.