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-terminal acetylated BAH domain of S.cerevisiae Sir3 bound to the nucleosome core particle revealed that the N-terminal ac...

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Autores principales: Arnaudo, Nadia, Fernández, Israel S., McLaughlin, Stephen H., Peak-Chew, Sew Y., Rhodes, Daniela, Martino, Fabrizio
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2013
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3818696/
https://www.ncbi.nlm.nih.gov/pubmed/23934150
http://dx.doi.org/10.1038/nsmb.2641
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author Arnaudo, Nadia
Fernández, Israel S.
McLaughlin, Stephen H.
Peak-Chew, Sew Y.
Rhodes, Daniela
Martino, Fabrizio
author_facet Arnaudo, Nadia
Fernández, Israel S.
McLaughlin, Stephen H.
Peak-Chew, Sew Y.
Rhodes, Daniela
Martino, Fabrizio
author_sort Arnaudo, Nadia
collection PubMed
description 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-terminal acetylated BAH domain of S.cerevisiae Sir3 bound to the nucleosome core particle revealed 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.
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spelling pubmed-38186962014-03-01 The N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particle Arnaudo, Nadia Fernández, Israel S. McLaughlin, Stephen H. Peak-Chew, Sew Y. Rhodes, Daniela Martino, Fabrizio Nat Struct Mol Biol Article 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-terminal acetylated BAH domain of S.cerevisiae Sir3 bound to the nucleosome core particle revealed 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. 2013-08-11 2013-09 /pmc/articles/PMC3818696/ /pubmed/23934150 http://dx.doi.org/10.1038/nsmb.2641 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Arnaudo, Nadia
Fernández, Israel S.
McLaughlin, Stephen H.
Peak-Chew, Sew Y.
Rhodes, Daniela
Martino, Fabrizio
The N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particle
title The N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particle
title_full The N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particle
title_fullStr The N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particle
title_full_unstemmed The N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particle
title_short The N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particle
title_sort n-terminal acetylation of sir3 stabilizes its binding to the nucleosome core particle
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3818696/
https://www.ncbi.nlm.nih.gov/pubmed/23934150
http://dx.doi.org/10.1038/nsmb.2641
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