dc.contributor.authorArnaudo, Nadia
dc.contributor.authorFernández, Israel S.
dc.contributor.authorMcLaughlin, Stephen H.
dc.contributor.authorPeak-Chew, Sew Y.
dc.contributor.authorRhodes, Daniela
dc.contributor.authorMartino, Fabrizio
dc.identifier.citationArnaudo, N., Fernández, I. S., McLaughlin, S. H., Peak-Chew, S. Y., Rhodes, D., & Martino, F. (2013). The N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particle. Nature structural & molecular biology, 20(9), 1119-1121.en_US
dc.description.abstractThe 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.en_US
dc.relation.ispartofseriesNature structural & molecular biologyen_US
dc.subjectDRNTU::Science::Biological sciences::Molecular biology
dc.titleThe N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particleen_US
dc.typeJournal Article
dc.contributor.schoolSchool of Biological Sciencesen_US

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