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 Km values, whereas small differences in kcat 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.

中文翻译：

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通过在组蛋白尾巴上掺入γ-硫赖氨酸来探索组蛋白酰基。

组蛋白赖氨酸乙酰基转移酶（KAT）催化乙酰基从乙酰辅酶A转移到组蛋白和非组蛋白中的赖氨酸残基上。在这里，我们报道了赖氨酸和γ-硫代赖氨酸（一种半胱氨酸衍生的赖氨酸模拟物）的表观遗传学乙酰化和相关酰化反应的生物分子研究，可以将其位点特异性引入组蛋白肽和组蛋白中。酶法测定表明，人KAT可催化具有赖氨酸和γ-硫代赖氨酸的组蛋白肽的有效乙酰化和丙酰化。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的Km值无法区分，而kcat值则存在微小差异。