ArticleMolecular and cellular biology2004
Budding yeast silencing complexes and regulation of Sir2 activity by protein-protein interactions.
Article in Molecular and cellular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 80 citations in OpenAlex.
- NADCells · 2025Review
- Unwrap RAP1's Mystery at Kinetoplastid Telomeres.Biomolecules · 2024Review
- An insight into the role of the N-terminal domain ofFrontiers in molecular biosciences · 2024Article
- Regulation of the heterochromatin spreading reaction byOpen biology · 2023Review
- A novel role of DOT1L in kidney diseases.Molecular biology reports · 2023Review
- Spreading-dependent or independent Sir2-mediated gene silencing in budding yeast.Genes & genomics · 2022Article
- Gene repression in S. cerevisiae-looking beyond Sir-dependent gene silencing.Current genetics · 2021Review
- A synthetic non-histone substrate to study substrate targeting by the Gcn5 HAT and sirtuin HDACs.The Journal of biological chemistry · 2019Article
- Discovery and Evolution of New Domains in Yeast Heterochromatin Factor Sir4 and Its Partner Esc1.Genome biology and evolution · 2019Article
- Recruitment and allosteric stimulation of a histone-deubiquitinating enzyme during heterochromatin assembly.The Journal of biological chemistry · 2018Article
- 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
- The Nuts and Bolts of Transcriptionally Silent Chromatin in Saccharomyces cerevisiae.Genetics · 2016Review
- Histone H3 N-terminal acetylation sites especially K14 are important for rDNA silencing and aging.Scientific reports · 2016Article
- Less is more: Nutrient limitation induces cross-talk of nutrient sensing pathways with NADFrontiers in biology · 2015Article
- Structural basis for allosteric, substrate-dependent stimulation of SIRT1 activity by resveratrol.Genes & development · 2015Article
- Affinity Purification of Protein Complexes Using TAP Tags.Methods in enzymology · 2015Article
- Regulation of NAD+ metabolism, signaling and compartmentalization in the yeast Saccharomyces cerevisiae.DNA repair · 2014Review
- Cross-talk between sirtuin and mammalian target of rapamycin complex 1 (mTORC1) signaling in the regulation of S6 kinase 1 (S6K1) phosphorylation.The Journal of biological chemistry · 2014Article
- Small-molecule allosteric activators of sirtuins.Annual review of pharmacology and toxicology · 2014Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Gene silencing in the budding yeast Saccharomyces cerevisiae requires the enzymatic activity of the Sir2 protein, a highly conserved NAD-dependent deacetylase. In order to study the activity of native Sir2, we purified and characterized two budding yeast Sir2 complexes: the Sir2/Sir4 complex, which mediates silencing at mating-type loci and at telomeres, and the RENT complex, which mediates silencing at the ribosomal DNA repeats. Analyses of the protein compositions of these complexes confirmed previously described interactions. We show that the assembly of Sir2 into native silencing complexes does not alter its selectivity for acetylated substrates, nor does it allow the deacetylation of nucleosomal histones. The inability of Sir2 complexes to deacetylate nucleosomes suggests that additional factors influence Sir2 activity in vivo. In contrast, Sir2 complexes show significant enhancement in their affinities for acetylated substrates and their sensitivities to the physiological inhibitor nicotinamide relative to recombinant Sir2. Reconstitution experiments showed that, for the Sir2/Sir4 complex, these differences stem from the physical interaction of Sir2 with Sir4. Finally, we provide evidence that the different nicotinamide sensitivities of Sir2/Sir4 and RENT in vitro could contribute to locus-specific differences in how Sir2 activity is regulated in vivo.
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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.