ArticleGenes & development2013
Structural basis for allosteric stimulation of Sir2 activity by Sir4 binding.
Article in Genes & development, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
24 citing papers in PubMed, 39 citations in OpenAlex.
- Physical interactions within the SIR heterochromatin complex potentiate inter-subunit communication and gene repression.Cell reports · 2026Article
- Tandem Allosteric Effects of Reactant and Product that Promote Deacetylation Cycles in Sir2.Journal of chemical information and modeling · 2025Article
- Transcriptional silencing in Saccharomyces cerevisiae: known unknowns.Epigenetics & chromatin · 2024Review
- Review
- Article
- Mechanism and design of allosteric activators of SIRT1.Protein & cell · 2023Article
- Molecular Mechanism of Sirtuin 1 Modulation by the AROS Protein.International journal of molecular sciences · 2022Article
- Article
- The Pleiotropic Function of Human Sirtuins as Modulators of Metabolic Pathways and Viral Infections.Cells · 2021Review
- The Sir4 H-BRCT domain interacts with phospho-proteins to sequester and repress yeast heterochromatin.The EMBO journal · 2019Article
- Depletion of Limiting rDNA Structural Complexes Triggers Chromosomal Instability and Replicative Aging ofGenetics · 2019Article
- Discovery and Evolution of New Domains in Yeast Heterochromatin Factor Sir4 and Its Partner Esc1.Genome biology and evolution · 2019Article
- Sirtuin activators and inhibitors: Promises, achievements, and challenges.Pharmacology & therapeutics · 2018Review
- During yeast chronological aging resveratrol supplementation results in a short-lived phenotype Sir2-dependent.Redox biology · 2017Article
- Variants of the Sir4 Coiled-Coil Domain Improve Binding to Sir3 for Heterochromatin Formation inG3 (Bethesda, Md.) · 2017Article
- Resveratrol serves as a protein-substrate interaction stabilizer in human SIRT1 activation.Scientific reports · 2016Article
- Determinants of Sir2-Mediated, Silent Chromatin Cohesion.Molecular and cellular biology · 2016Article
- The Nuts and Bolts of Transcriptionally Silent Chromatin in Saccharomyces cerevisiae.Genetics · 2016Review
- Sumoylation of Sir2 differentially regulates transcriptional silencing in yeast.Nucleic acids research · 2015Article
- Crystallographic structure of a small molecule SIRT1 activator-enzyme complex.Nature communications · 2015Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
Abstract
The budding yeast Sir2 (silent information regulator 2) protein is the founding member of the sirtuin family of NAD-dependent histone/protein deacetylases. Its function in transcriptional silencing requires both the highly conserved catalytic domain and a poorly understood N-terminal regulatory domain (Sir2N). We determined the structure of Sir2 in complex with a fragment of Sir4, a component of the transcriptional silencing complex in Saccharomyces cerevisiae. The structure shows that Sir4 is anchored to Sir2N and contacts the interface between the Sir2N and the catalytic domains through a long loop. We discovered that the interaction between the Sir4 loop and the interdomain interface in Sir2 is critical for allosteric stimulation of the deacetylase activity of Sir2. These results bring to light the structure and function of the regulatory domain of Sir2, and the knowledge should be useful for understanding allosteric regulation of sirtuins in general.
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Registered trials
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.