Nα-acetylated Sir3 stabilizes the conformation of a nucleosome-binding loop in the BAH domain.
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.
1] National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China. [2] University of Chinese Academy of Sciences, Beijing, China. [3].
Dongxue
D
Yang
Qianglin
Q
Fang
Mingzhu
M
Wang
Ren
R
Ren
Hong
H
Wang
Meng
M
He
Youwei
Y
Sun
Na
N
Yang
Rui-Ming
RM
Xu
D000107:Acetylation; D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D020868:Gene Silencing; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009707:Nucleosomes / Q000378:metabolism*; D011487:Protein Conformation; D054730:Protein Interaction Domains and Motifs; D055550:Protein Stability; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism; D038281:Silent Information Regulator Proteins, Saccharomyces cerevisiae / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D055672:Static Electricity
D009707:Nucleosomes; D011994:Recombinant Proteins; C084122:SIR3 protein, S cerevisiae; D038281:Silent Information Regulator Proteins, Saccharomyces cerevisiae