The N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particle.
The N-terminal acetylation of Sir3 is essential for heterochromatin establishment and maintenance in yeast, but its mechanism of action is unknown. The crystal structure of the N-terminally acetylated BAH domain of Saccharomyces cerevisiae Sir3 bound to the nucleosome core particle reveals that the N-terminal acetylation stabilizes the interaction of Sir3 with the nucleosome. Additionally, we present a new method for the production of protein-nucleosome complexes for structural analysis.
Structural Studies Division, Medical Research Council-Laboratory of Molecular Biology, Cambridge, UK.
Nadia
N
Arnaudo
Israel S
IS
Fernández
Stephen H
SH
McLaughlin
Sew Y
SY
Peak-Chew
Daniela
D
Rhodes
Fabrizio
F
Martino
D000107:Acetylation; D018360:Crystallography, X-Ray; D046911:Macromolecular Substances / Q000737:chemistry / Q000302:isolation & purification; D008958:Models, Molecular; 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
D046911:Macromolecular Substances; D009707:Nucleosomes; D011994:Recombinant Proteins; C084122:SIR3 protein, S cerevisiae; D038281:Silent Information Regulator Proteins, Saccharomyces cerevisiae