ArticleNature structural & molecular biology2013
Nα-acetylated Sir3 stabilizes the conformation of a nucleosome-binding loop in the BAH domain.
Article in Nature structural & molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed.
- Physical interactions within the SIR heterochromatin complex potentiate inter-subunit communication and gene repression.Cell reports · 2026Article
- N-terminal acetylation controls multiple functional aspects of the influenza A virus ribonuclease PA-X.Journal of virology · 2026Article
- N-terminal acetylation controls multiple functional aspects of the influenza A virus ribonuclease PA-X.bioRxiv : the preprint server for biology · 2025Article
- InPathogens (Basel, Switzerland) · 2025Article
- Illuminating the impact of N-terminal acetylation: from protein to physiology.Nature communications · 2025Review
- Post-translational modifications in the Protein Data Bank.Acta crystallographica. Section D, Structural biology · 2024Review
- Article
- Domain Structure of the Dnmt1, Dnmt3a, and Dnmt3b DNA Methyltransferases.Advances in experimental medicine and biology · 2022Article
- Transcriptome characteristics during cell wall formation of endosperm cellularization and embryo differentiation inFrontiers in plant science · 2022Article
- How important is the N-terminal acetylation of alpha-synuclein for its function and aggregation into amyloids?Frontiers in neuroscience · 2022Review
- Hydroxylation of the Acetyltransferase NAA10 Trp38 Is Not an Enzyme-Switch in Human Cells.International journal of molecular sciences · 2021Article
- Molecular mechanism of N-terminal acetylation by the ternary NatC complex.Structure (London, England : 1993) · 2021Article
- Article
- Coupling of H3K27me3 recognition with transcriptional repression through the BAH-PHD-CPL2 complex in Arabidopsis.Nature communications · 2020Article
- Structural basis for nucleosome-mediated inhibition of cGAS activity.Cell research · 2020Article
- Divergent architecture of the heterotrimeric NatC complex explains N-terminal acetylation of cognate substrates.Nature communications · 2020Article
- Article
- N-terminal acetylation of actin by NAA80 is essential for structural integrity of the Golgi apparatus.Experimental cell research · 2020Article
- N-Terminal Acetylation Stabilizes SIGMA FACTOR BINDING PROTEIN1 Involved in Salicylic Acid-Primed Cell Death.Plant physiology · 2020Article
- Molecular basis for N-terminal acetylation by human NatE and its modulation by HYPK.Nature communications · 2020Article
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9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In Saccharomyces cerevisiae, acetylation of the Sir3 N terminus is important for transcriptional silencing. This covalent modification promotes the binding of the Sir3 BAH domain to the nucleosome, but a mechanistic understanding of this phenomenon is lacking. By X-ray crystallography, we show here that the acetylated N terminus of Sir3 does not interact with the nucleosome directly. Instead, it stabilizes a nucleosome-binding loop in the BAH domain.
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