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The N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particle

DOI: 10.1038/nsmb.2641 DOI Help
PMID: 23934150 PMID Help

Authors: Nadia Arnaudo (Medical Research Council-Laboratory of Molecular Biology) , Israel S. Fernandez (Medical Research Council-Laboratory of Molecular Biology) , Stephen H. Mclaughlin (Medical Research Council-Laboratory of Molecular Biology) , Sew Y. Peak-Chew (Medical Research Council-Laboratory of Molecular Biology) , Daniela Rhodes (Medical Research Council-Laboratory of Molecular Biology) , Fabrizio Martino (Medical Research Council-Laboratory of Molecular Biology)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Structural & Molecular Biology

State: Published (Approved)
Published: August 2013

Abstract: 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.

Journal Keywords: Crystallography; X-Ray; Macromolecular; Models; Molecular; Mutagenesis; Site-Directed; Nucleosomes; Protein; Recombinant; Saccharomyces; Silent; Saccharomyces; Static Electricity

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: I24-Microfocus Macromolecular Crystallography

Added On: 30/08/2013 10:28

Discipline Tags:

Biochemistry Genetics Chemistry Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)