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PMID:10811920
| Citation |
Landry, J, Sutton, A, Tafrov, ST, Heller, RC, Stebbins, J, Pillus, L and Sternglanz, R (2000) The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases. Proc. Natl. Acad. Sci. U.S.A. 97:5807-11 |
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| Abstract |
Homologs of the chromatin-bound yeast silent information regulator 2 (SIR2) protein are found in organisms from all biological kingdoms. SIR2 itself was originally discovered to influence mating-type control in haploid cells by locus-specific transcriptional silencing. Since then, SIR2 and its homologs have been suggested to play additional roles in suppression of recombination, chromosomal stability, metabolic regulation, meiosis, and aging. Considering the far-ranging nature of these functions, a major experimental goal has been to understand the molecular mechanism(s) by which this family of proteins acts. We report here that members of the SIR2 family catalyze an NAD-nicotinamide exchange reaction that requires the presence of acetylated lysines such as those found in the N termini of histones. Significantly, these enzymes also catalyze histone deacetylation in a reaction that absolutely requires NAD, thereby distinguishing them from previously characterized deacetylases. The enzymes are active on histone substrates that have been acetylated by both chromatin assembly-linked and transcription-related acetyltransferases. Contrary to a recent report, we find no evidence that these proteins ADP-ribosylate histones. Discovery of an intrinsic deacetylation activity for the conserved SIR2 family provides a mechanism for modifying histones and other proteins to regulate transcription and diverse biological processes. |
| Links |
PubMed PMC18515 Online version:10.1073/pnas.110148297 |
| Keywords |
Acetylation; Adenosine Diphosphate Ribose/metabolism; Animals; Chickens; Fungal Proteins/genetics; Fungal Proteins/physiology; Gene Silencing/physiology; Histone Deacetylases/genetics; Histone Deacetylases/physiology; Histones/chemistry; Histones/metabolism; Lysine/metabolism; Multigene Family; NAD/metabolism; Niacinamide/metabolism; Protein Processing, Post-Translational; Recombinant Fusion Proteins/metabolism; Saccharomyces cerevisiae/enzymology; Saccharomyces cerevisiae/genetics; Silent Information Regulator Proteins, Saccharomyces cerevisiae; Sirtuin 2; Sirtuins; Trans-Activators/genetics; Trans-Activators/physiology |
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Significance
Annotations
| Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
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