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鉴定 Sirtuin6 的新型相互作用伙伴。

Identification of novel interacting partners of Sirtuin6.

机构信息

Platform Technology Sciences, GlaxoSmithKline, Stevenage, Hertfordshire, United Kingdom.

出版信息

PLoS One. 2012;7(12):e51555. doi: 10.1371/journal.pone.0051555. Epub 2012 Dec 11.

Abstract

SIRT6 is a member of the Sirtuin family of histone deacetylases that has been implicated in inflammatory, aging and metabolic pathways. Some of its actions have been suggested to be via physical interaction with NFκB and HIF1α and transcriptional regulation through its histone deacetylase activity. Our previous studies have investigated the histone deacetylase activity of SIRT6 and explored its ability to regulate the transcriptional responses to an inflammatory stimulus such as TNFα. In order to develop a greater understanding of SIRT6 function we have sought to identify SIRT6 interacting proteins by both yeast-2-hybrid and co-immunoprecipitation studies. We report a number of interacting partners which strengthen previous findings that SIRT6 functions in base excision repair (BER), and novel interactors which suggest a role in nucleosome and chromatin remodeling, the cell cycle and NFκB biology.

摘要

SIRT6 是组蛋白去乙酰化酶 Sirtuin 家族的成员,它与炎症、衰老和代谢途径有关。它的一些作用被认为是通过与 NFκB 和 HIF1α 的物理相互作用以及通过其组蛋白去乙酰化酶活性进行转录调节。我们之前的研究调查了 SIRT6 的组蛋白去乙酰化酶活性,并探索了它调节对 TNFα 等炎症刺激的转录反应的能力。为了更深入地了解 SIRT6 的功能,我们通过酵母双杂交和共免疫沉淀研究来寻找 SIRT6 的相互作用蛋白。我们报告了一些相互作用的伙伴,这些伙伴加强了 SIRT6 在碱基切除修复(BER)中发挥作用的先前发现,以及一些新的相互作用伙伴,这表明 SIRT6 在核小体和染色质重塑、细胞周期和 NFκB 生物学中发挥作用。

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