Please use this identifier to cite or link to this item:
https://hdl.handle.net/10356/98638
Title: | The N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particle | Authors: | Arnaudo, Nadia Rhodes, Daniela Martino, Fabrizio Fernández, Israel S. McLaughlin, Stephen H. Peak-Chew, Sew Y. |
Keywords: | DRNTU::Science::Biological sciences::Molecular biology | Issue Date: | 2013 | Source: | 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. | Series/Report no.: | Nature structural & molecular biology | 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. | URI: | https://hdl.handle.net/10356/98638 http://hdl.handle.net/10220/17646 |
DOI: | 10.1038/nsmb.2641 | Schools: | School of Biological Sciences | Fulltext Permission: | none | Fulltext Availability: | No Fulltext |
Appears in Collections: | SBS Journal Articles |
SCOPUSTM
Citations
5
65
Updated on Mar 16, 2024
Web of ScienceTM
Citations
5
64
Updated on Oct 25, 2023
Page view(s) 10
790
Updated on Mar 18, 2024
Google ScholarTM
Check
Altmetric
Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.