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- W2000651503 abstract "The yeast Sir2/3/4 complex forms a heterochromatin-like structure that represses transcription. The proteins nucleate at silencers and spread distally, utilizing the Sir2 NAD(+)-dependent histone deacetylase activity and the affinity of Sir3/4 for deacetylated histone tails. A by-product of the Sir2 reaction, O-acetyl-ADP-ribose (OAADPr), is thought to aid spreading by binding one of the Sir proteins. We developed a protein chimera approach to reexamine the contributions of Sir2. We show that a Sir3 chimera-bearing Hos3, an unrelated NAD(+)-independent histone deacetylase, substitutes for Sir2 in silencing. Sir3-Hos3 operates within the Sir pathway, spreading while deacetylating histones. Moreover, the chimera represses HM loci in strains lacking all five OAADPr-producing deacetylases, indicating that OAADPr is not necessary for silencing. Repression by a Hos3 hybrid bearing the targeting motifs of Sir2 shows that targeting doesn't require the Sir2 reaction. Together, these data demonstrate that protein deacetylation is the only essential function of Sir2 in creating silenced chromatin." @default.
- W2000651503 created "2016-06-24" @default.
- W2000651503 creator A5046400480 @default.
- W2000651503 creator A5049896634 @default.
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- W2000651503 date "2008-09-01" @default.
- W2000651503 modified "2023-10-12" @default.
- W2000651503 title "Bypassing Sir2 and O-Acetyl-ADP-Ribose in Transcriptional Silencing" @default.
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- W2000651503 doi "https://doi.org/10.1016/j.molcel.2008.06.020" @default.
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