Department of Physics, Chemistry and Pharmacy, University of Southern Denmark, Campusvej 55, 5230 Odense, Denmark.
Bioconjug Chem. 2020 Mar 18;31(3):844-851. doi: 10.1021/acs.bioconjchem.0c00012. Epub 2020 Feb 27.
Histone lysine acetyltransferases (KATs) catalyze the transfer of the acetyl group from acetyl Coenzyme A to lysine residues in histones and nonhistone proteins. Here, we report biomolecular studies on epigenetic acetylation and related acylation reactions of lysine and γ-thialysine, a cysteine-derived lysine mimic, which can be site-specifically introduced to histone peptides and histone proteins. Enzyme assays demonstrate that human KATs catalyze an efficient acetylation and propionylation of histone peptides that possess lysine and γ-thialysine. Enzyme kinetics analyses reveal that lysine- and γ-thialysine-containing histone peptides exhibit indistinguishable values, whereas small differences in values were observed. This work highlights that γ-thialysine may act as a representative and easily accessible lysine mimic for chemical and biochemical examinations of post-translationally modified histones.
组蛋白赖氨酸乙酰转移酶（KATs）催化乙酰辅酶 A 上的乙酰基转移到组蛋白和非组蛋白蛋白质中的赖氨酸残基上。在这里，我们报告了关于赖氨酸和γ-硫代赖氨酸（一种半胱氨酸衍生的赖氨酸类似物）的表观遗传乙酰化和相关酰化反应的生物分子研究，γ-硫代赖氨酸可以在组蛋白肽和组蛋白蛋白中进行特异性引入。酶促实验表明，人类 KATs 可有效地催化具有赖氨酸和γ-硫代赖氨酸的组蛋白肽的乙酰化和丙酰化。酶动力学分析表明，含有赖氨酸和γ-硫代赖氨酸的组蛋白肽表现出相同的 值，而在 值上观察到较小的差异。这项工作强调了γ-硫代赖氨酸可以作为一种代表性且易于获得的赖氨酸类似物，用于研究翻译后修饰的组蛋白的化学和生物化学。
