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PMID:19217406
| Citation |
Martino, F, Kueng, S, Robinson, P, Tsai-Pflugfelder, M, van Leeuwen, F, Ziegler, M, Cubizolles, F, Cockell, MM, Rhodes, D and Gasser, SM (2009) Reconstitution of yeast silent chromatin: multiple contact sites and O-AADPR binding load SIR complexes onto nucleosomes in vitro. Mol. Cell 33:323-34 |
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| Abstract |
At yeast telomeres and silent mating-type loci, chromatin assumes a higher-order structure that represses transcription by means of the histone deacetylase Sir2 and structural proteins Sir3 and Sir4. Here, we present a fully reconstituted system to analyze SIR holocomplex binding to nucleosomal arrays. Purified Sir2-3-4 heterotrimers bind chromatin, cooperatively yielding a stable complex of homogeneous molecular weight. Remarkably, Sir2-3-4 also binds naked DNA, reflecting the strong, albeit nonspecific, DNA-binding activity of Sir4. The binding of Sir3 to nucleosomes is sensitive to histone H4 N-terminal tail removal, while that of Sir2-4 is not. Dot1-mediated methylation of histone H3K79 reduces the binding of both Sir3 and Sir2-3-4. Additionally, a byproduct of Sir2-mediated NAD hydrolysis, O-acetyl-ADP-ribose, increases the efficiency with which Sir3 and Sir2-3-4 bind nucleosomes. Thus, in small cumulative steps, each Sir protein, unmodified histone domains, and contacts with DNA contribute to the stability of the silent chromatin complex. |
| Links |
PubMed Online version:10.1016/j.molcel.2009.01.009 |
| Keywords |
Binding Sites; Chromatin/metabolism; Histone Deacetylases/isolation & purification; Histone Deacetylases/metabolism; Models, Biological; Models, Molecular; Nucleosomes/metabolism; O-Acetyl-ADP-Ribose/metabolism; Saccharomyces cerevisiae/genetics; Saccharomyces cerevisiae/metabolism; Silent Information Regulator Proteins, Saccharomyces cerevisiae/isolation & purification; Silent Information Regulator Proteins, Saccharomyces cerevisiae/metabolism; Sirtuin 2; Sirtuins/isolation & purification; Sirtuins/metabolism |
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