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Publication Abstract from PubMed

In Saccharomyces cerevisiae, acetylation of the Sir3 N terminus is important for transcriptional silencing. This covalent modification promotes the binding of the Sir3 BAH domain to the nucleosome, but a mechanistic understanding of this phenomenon is lacking. By X-ray crystallography, we show here that the acetylated N terminus of Sir3 does not interact with the nucleosome directly. Instead, it stabilizes a nucleosome-binding loop in the BAH domain.

Nalpha-acetylated Sir3 stabilizes the conformation of a nucleosome-binding loop in the BAH domain.,Yang D, Fang Q, Wang M, Ren R, Wang H, He M, Sun Y, Yang N, Xu RM Nat Struct Mol Biol. 2013 Aug 11. doi: 10.1038/nsmb.2637. PMID:23934152^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.