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

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...

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Main Authors: Arnaudo, Nadia, Rhodes, Daniela, Martino, Fabrizio, Fernández, Israel S., McLaughlin, Stephen H., Peak-Chew, Sew Y.
Other Authors: School of Biological Sciences
Format: Article
Language:English
Published: 2013
Subjects:
DRNTU::Science::Biological sciences::Molecular biology
Online Access:https://hdl.handle.net/10356/98638
http://hdl.handle.net/10220/17646
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Institution: Nanyang Technological University
Language: English
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spelling sg-ntu-dr.10356-986382022-02-16T16:28:57Z The N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particle Arnaudo, Nadia Rhodes, Daniela Martino, Fabrizio Fernández, Israel S. McLaughlin, Stephen H. Peak-Chew, Sew Y. School of Biological Sciences DRNTU::Science::Biological sciences::Molecular biology 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. 2013-11-15T02:12:40Z 2019-12-06T19:58:00Z 2013-11-15T02:12:40Z 2019-12-06T19:58:00Z 2013 2013 Journal Article Arnaudo, 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. https://hdl.handle.net/10356/98638 http://hdl.handle.net/10220/17646 10.1038/nsmb.2641 23934150 en Nature structural & molecular biology
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic DRNTU::Science::Biological sciences::Molecular biology
spellingShingle DRNTU::Science::Biological sciences::Molecular biology
Arnaudo, Nadia
Rhodes, Daniela
Martino, Fabrizio
Fernández, Israel S.
McLaughlin, Stephen H.
Peak-Chew, Sew Y.
The N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particle
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-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.
author2 School of Biological Sciences
author_facet School of Biological Sciences
Arnaudo, Nadia
Rhodes, Daniela
Martino, Fabrizio
Fernández, Israel S.
McLaughlin, Stephen H.
Peak-Chew, Sew Y.
format Article
author Arnaudo, Nadia
Rhodes, Daniela
Martino, Fabrizio
Fernández, Israel S.
McLaughlin, Stephen H.
Peak-Chew, Sew Y.
author_sort Arnaudo, Nadia
title 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_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_sort n-terminal acetylation of sir3 stabilizes its binding to the nucleosome core particle
publishDate 2013
url https://hdl.handle.net/10356/98638
http://hdl.handle.net/10220/17646
_version_ 1725985546649468928

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