SIRT6 exhibits nucleosome-dependent deacetylase activity

Reuven Gil; Shaul Barth; Yariv Kanfi; Haim Y. Cohen

doi:10.1093/nar/gkt642

SIRT6 exhibits nucleosome-dependent deacetylase activity

Reuven Gil, Shaul Barth, Yariv Kanfi, Haim Y. Cohen

The Mina and Everard Goodman Faculty of Life Sciences - at Bar-Ilan University

Bar-Ilan University

Research output: Contribution to journal › Article › peer-review

100 Scopus citations

Abstract

The SIRT6 deacetylase is a key regulator of mammalian genome stability, metabolism and lifespan. Previous studies indicated that SIRT6 exhibits poor deacetylase activity in vitro. Here, we explored the specific conditions that allow SIRT6 to function as a significant deacetylase. We show that SIRT6 associates with the nucleosome and deacetylates histones H3 and H4 when they are packaged as nucleosomes, but not as free histones. In contrast, SIRT1 shows the opposite characteristics. Thus, our results show that SIRT6 activity is nucleosome dependent, and suggest that its binding to the nucleosome might convert it into an active structure.

Original language	English
Pages (from-to)	8537-8545
Number of pages	9
Journal	Nucleic Acids Research
Volume	41
Issue number	18
DOIs	https://doi.org/10.1093/nar/gkt642
State	Published - Oct 2013

Bibliographical note

Funding Information:
Israel Science Foundation, I-Core foundation, Israeli Ministry of Health and the ERC: European Research Council. Funding for open access charge: ERC.

Funding

Israel Science Foundation, I-Core foundation, Israeli Ministry of Health and the ERC: European Research Council. Funding for open access charge: ERC.

Funders	Funder number
I-Core Foundation
Seventh Framework Programme	242763
European Commission
Israel Science Foundation
Ministry of Health, State of Israel

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abstract = "The SIRT6 deacetylase is a key regulator of mammalian genome stability, metabolism and lifespan. Previous studies indicated that SIRT6 exhibits poor deacetylase activity in vitro. Here, we explored the specific conditions that allow SIRT6 to function as a significant deacetylase. We show that SIRT6 associates with the nucleosome and deacetylates histones H3 and H4 when they are packaged as nucleosomes, but not as free histones. In contrast, SIRT1 shows the opposite characteristics. Thus, our results show that SIRT6 activity is nucleosome dependent, and suggest that its binding to the nucleosome might convert it into an active structure.",

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SIRT6 exhibits nucleosome-dependent deacetylase activity

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