Sirtuins 1 and 2 Are Universal Histone Deacetylases

ACS Chemical Biology
Willie W HsuWenshe R Liu

Abstract

Lysine acetylation serves as an epigenetic marker for myriad cellular processes, such as signaling, differentiation, DNA repair, angiogenesis, and the like. Sirtuin 1 (SIRT1) and sirtuin 2 (SIRT2) are NAD(+)-dependent histone deacetylases that operate as post-translational regulators for the deacetylation of acetyllysine. Here, we discuss the ability for SIRT1 and SIRT2 to deacetylate monoacetylated histone H3 on two separate architectures-the peptide and the nucleosome. In addition, we analyze the site-specificity of SIRT1 and SIRT2 on 10 different monoacetylated histone H3 nucleosomes. By utilizing a rapid screening array, SIRT1 and SIRT2 were found to demonstrate heightened enzymatic activity when incubated with nucleosomal substrates over their peptide counterparts. These two enzymes displayed little site-specificity among the acetyl-nucleosomes screened, contrary to previous expectations, as well. The implication of the overall nonspecificity of SIRT1 and SIRT2 on the nucleosome suggests that these sirtuin enzymes have an adaptive nature, harnessing an ability to respond to various cellular situations, rather than an enzyme specifically designed for a particular task or function.

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Citations

May 7, 2016·ACS Chemical Biology·Wesley Wei WangWenshe R Liu
Oct 21, 2016·Journal of Pineal Research·Rüdiger Hardeland
Jan 31, 2017·Journal of Medicinal Chemistry·Sandeep SundriyalMatthew J Fuchter
Jan 18, 2017·Medicinal Research Reviews·Matthias SchiedelManfred Jung
Sep 14, 2017·RNA Biology·Aerin YangHee-Sung Park
Jul 20, 2016·Hypertension·Jessica L FryFrancesca Seta
Jan 22, 2019·Frontiers in Genetics·Lyubomir I AftanasSergei P Kovalenko
Jan 23, 2019·JCI Insight·Yong Gyu LeeMegan N Ballinger
Jan 8, 2020·International Journal of Molecular Sciences·Rebeca González-FernándezJulio Ávila
Nov 3, 2017·Chembiochem : a European Journal of Chemical Biology·Vangmayee SharmaWenshe R Liu
Jan 18, 2019·Journal of the American Chemical Society·Wesley Wei WangWenshe Ray Liu

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