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The N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particle
DOI:
10.1038/nsmb.2641
PMID:
23934150
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)