ArticleProceedings of the National Academy of Sciences of the United States of America2003
Histone deacetylation by Sir2 generates a transcriptionally repressed nucleoprotein complex.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 38 citations in OpenAlex.
- Metabolic and post-translational modifications in sepsis-associated immune dysfunction: a conceptual framework.Frontiers in immunology · 2026Review
- Tandem Allosteric Effects of Reactant and Product that Promote Deacetylation Cycles in Sir2.Journal of chemical information and modeling · 2025Article
- Human OGG1 activity in nucleosomes is facilitated by transient unwrapping of DNA and is influenced by the local histone environment.DNA repair · 2017Article
- Embedding the Future of Regenerative Medicine into the Open Epigenomic Landscape of Pluripotent Human Embryonic Stem Cells.Annual research & review in biology · 2013Article
- Human Stem Cell Derivatives Retain More Open Epigenomic Landscape When Derived from Pluripotent Cells than from Tissues.Journal of regenerative medicine · 2013Article
- An Engraftable Human Embryonic Stem Cell Neuronal Lineage-Specific Derivative Retains Embryonic Chromatin Plasticity for Scale-Up CNS Regeneration.Journal of regenerative medicine & tissue engineering · 2012Article
- MicroRNA Profiling Reveals Distinct Mechanisms Governing Cardiac and Neural Lineage-Specification of Pluripotent Human Embryonic Stem Cells.Journal of stem cell research & therapy · 2012Article
- The Dynamics of Global Chromatin Remodeling are Pivotal for Tracking the Normal Pluripotency of Human Embryonic Stem Cells.Anatomy & physiology : current research · 2012Article
- Molecular mechanisms of aging and immune system regulation in Drosophila.International journal of molecular sciences · 2012Review
- A role for histone H4K16 hypoacetylation in Saccharomyces cerevisiae kinetochore function.Genetics · 2011Article
- GAPDH mediates nitrosylation of nuclear proteins.Nature cell biology · 2010Article
- Silenced yeast chromatin is maintained by Sir2 in preference to permitting histone acetylations for efficient NER.Nucleic acids research · 2010Article
- Reconstitution of heterochromatin-dependent transcriptional gene silencing.Molecular cell · 2009Article
- Corepressive action of CBP on androgen receptor transactivation in pericentric heterochromatin in a Drosophila experimental model system.Molecular and cellular biology · 2009Article
- Chromatin: linking structure and function in the nucleolus.Chromosoma · 2009Review
- SIRT1 negatively regulates HDAC1-dependent transcriptional repression by the RBP1 family of proteins.Oncogene · 2008Article
- Budding yeast silencing complexes and regulation of Sir2 activity by protein-protein interactions.Molecular and cellular biology · 2004Article
- Silent information regulator 2 potentiates Foxo1-mediated transcription through its deacetylase activity.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Sir2 is an NAD-dependent histone deacetylase required for transcriptional silencing. To study the mechanism of Sir2 function, we examined the biochemical properties of purified recombinant Drosophila Sir2 (dSir2). First, we performed histone deacetylation assays and found that dSir2 deacetylates a broad range of acetylated lysine residues. We then carried out in vitro transcription experiments and observed that dSir2 does not repress transcription with either naked DNA templates or chromatin assembled from native (and mostly unacetylated) histones. It was possible, however, that repression by dSir2 requires an acetylated histone substrate. We therefore tested the transcriptional effects of dSir2 with native histones that were hyperacetylated by treatment with acetic anhydride. Assembly of the hyperacetylated histones onto DNA yields a soluble histone-DNA complex that differs from canonical nucleosomal chromatin. With this hyperacetylated histone-DNA complex, we observed potent (50- to 100-fold) NAD-dependent transcriptional repression by purified dSir2. In contrast, repression by dSir2 was not observed in parallel experiments in which histones were hyperpropionylated with propionic anhydride. We also found that dSir2 mediates the formation of a nuclease-resistant fast-sedimenting histone-DNA complex in an NAD-dependent manner. Unlike dSir2, the dHDAC1 deacetylase does not strongly repress transcription or generate a nuclease-resistant histone-DNA complex. Furthermore, with yeast Sir2, the transcriptional repression we observe correlates with deacetylation activity in vitro and silencing activity in vivo. These findings suggest that deacetylation by Sir2 causes a conformational change or rearrangement of histones into a transcriptionally repressive chromatin structure.
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