确定赖氨酸甲基转移酶的底物特异性
Determining the Substrate Specificity of Lysine Methyltransferases.
作者信息
Hanquier Jocelyne N, Berryhill Christine A, Cornett Evan M
机构信息
Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN, USA.
Stark Neurosciences Research Institute, Indiana University School of Medicine, Indianapolis, IN, USA.
出版信息
Methods Mol Biol. 2025;2919:241-250. doi: 10.1007/978-1-0716-4486-7_13.
Lysine methyltransferases (KMTs) catalyze mono-, di-, and tri-methylation on histone and non-histone proteins. Determining the substrate specificity of KMTs is a critical task. This chapter outlines a method to perform highly sensitive in vitro methyltransferase assays on peptide substrates. In addition to comparing peptide substrates from histone or non-histone proteins, we also describe the use of a lysine-oriented peptide library (K-OPL) to generate high-resolution substrate specificity profiles for KMTs.
赖氨酸甲基转移酶（KMTs）催化组蛋白和非组蛋白上的单甲基化、二甲基化和三甲基化。确定KMTs的底物特异性是一项关键任务。本章概述了一种在肽底物上进行高度灵敏的体外甲基转移酶测定的方法。除了比较来自组蛋白或非组蛋白的肽底物外，我们还描述了使用赖氨酸导向肽库（K-OPL）来生成KMTs的高分辨率底物特异性图谱。
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