Protein Structure Group, Korea Basic Science Institute, Cheongju-Si, South Korea.
Department of Bio-Analytical Science, University of Science and Technology, Daejon, South Korea.
FEBS J. 2018 Apr;285(7):1277-1289. doi: 10.1111/febs.14404. Epub 2018 Mar 4.
Nonenzymatic acetylation of Lys side chains (Lys-SCs) by various in vivo reactive molecules has been suggested to play novel regulatory roles. Ubiquitin (UB) has seven Lys residues that are utilized for synthesis of specific poly-UB chains. To understand the nature of these Lys-SC modifications, the chemical acetylation rate and pK and Hill coefficient of each UB-Lys-SC were measured. Mutagenesis studies combined with the determination of activation energy indicated that specific neighboring residues of the Lys-SCs have a potential catalytic activity during nonenzymatic acetylation. Based on the shared chemistry between nonenzymatic Lys acetylation and ubiquitylation, the characterized chemical properties of the UB-Lys-SCs could be a reference for deciphering both mechanisms. Our NMR approaches could be useful for studying general nonenzymatic Lys acylations of various proteins.
非酶促乙酰化赖氨酸侧链（Lys-SCs）由各种体内反应性分子已经被提出发挥新的调节作用。泛素（UB）有七个赖氨酸残基被用于合成特定的多泛素链。为了了解这些 Lys-SC 修饰的性质，测量了每个 UB-Lys-SC 的化学乙酰化速率和 pK 值及 Hill 系数。突变研究结合激活能的测定表明，Lys-SC 的特定相邻残基在非酶促乙酰化过程中具有潜在的催化活性。基于非酶促赖氨酸乙酰化和泛素化之间的共享化学性质，所鉴定的 UB-Lys-SC 的化学性质可以作为破译这两种机制的参考。我们的 NMR 方法可用于研究各种蛋白质的一般非酶促 Lys 酰化。
