生物正交化学
组蛋白
化学生物学
蛋白质组
组合化学
赖氨酸
化学
蛋白质组学
计算生物学
翻译后修饰
生物
生物化学
基因
氨基酸
点击化学
酶
作者
Yanan Sun,Yanchi Chen,Tao Peng
出处
期刊:Chemical Science
[The Royal Society of Chemistry]
日期:2022-01-01
卷期号:13 (20): 6019-6027
被引量:18
摘要
l-Lactylation is a recently discovered post-translational modification occurring on histone lysine residues to regulate gene expression. However, the substrate scope of lactylation, especially that in non-histone proteins, remains unknown, largely due to the limitations of current methods for analyzing lactylated proteins. Herein, we report an alkynyl-functionalized bioorthogonal chemical reporter, YnLac, for the detection and identification of protein lactylation in mammalian cells. Our in-gel fluorescence and chemical proteomic analyses show that YnLac is metabolically incorporated into lactylated proteins and directly labels known lactylated lysines of histones. We further apply YnLac to the proteome-wide profiling of lactylation, revealing many novel modification sites in non-histone proteins for the first time. Moreover, we demonstrate that lactylation of a newly identified substrate protein PARP1 regulates its ADP-ribosylation activity. Our study thus provides a powerful chemical tool for characterizing protein lactylation and greatly expands our understanding of substrate proteins and functions of this new modification.
科研通智能强力驱动
Strongly Powered by AbleSci AI