Synthetic and Functional Biomolecules Center, Beijing National Laboratory for Molecular Sciences, Key Laboratory of Bioorganic Chemistry and Molecular Engineering of Ministry of Education, College of Chemistry and Molecular Engineering, Peking University , Beijing 100871, China.
Department of Chemistry, The University of Hong Kong , Pokfulam Road, Hong Kong, China.
J Am Chem Soc. 2017 May 17;139(19):6522-6525. doi: 10.1021/jacs.7b01431. Epub 2017 May 8.
Posttranslational modifications (PTMs) of lysine are crucial histone marks that regulate diverse biological processes. The functional roles and regulation mechanism of many newly identified lysine PTMs, however, remain yet to be understood. Here we report a photoaffinity crotonyl lysine (Kcr) analogue that can be genetically and site-specifically incorporated into histone proteins. This, in conjunction with the genetically encoded photo-lysine as a "control probe", enables the capture and identification of enzymatic machinery and/or effector proteins for histone lysine crotonylation.
赖氨酸的翻译后修饰（PTMs）是调节多种生物过程的关键组蛋白标记。然而，许多新鉴定的赖氨酸 PTM 的功能作用和调控机制尚不清楚。在这里，我们报告了一种光亲和性巴豆酰赖氨酸（Kcr）类似物，它可以在遗传上和位点特异性地掺入组蛋白蛋白中。结合遗传编码的光赖氨酸作为“对照探针”，可以捕获和鉴定组蛋白赖氨酸巴豆酰化的酶机制和/或效应蛋白。
