Photo-lysine captures proteins that bind lysine post-translational modifications

被引：0
|
作者：
Yang, Tangpo [1 ]
Li, Xiao-Meng [1 ]
Bao, Xiucong [1 ]
Fung, Yi Man Eva [1 ]
Li, Xiang David [1 ]
机构：
[1] Univ Hong Kong, Dept Chem, Pokfulam Rd, Hong Kong, Hong Kong, Peoples R China
来源：
NATURE CHEMICAL BIOLOGY | 2016年 / 12卷 / 02期
关键词：
HISTONE; METHYLTRANSFERASE; IDENTIFICATION; PURIFICATION; RECOGNITION; METHYLATION; MECHANISM; CELLS;
D O I：
10.1038/NCHEMBIO.1990
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Post-translational modifications (PTMs) have key roles in regulating protein-protein interactions in living cells. However, it remains a challenge to identify these PTM-mediated interactions. Here we develop a new lysine-based photo-reactive amino acid, termed photo-lysine. We demonstrate that photo-lysine, which is readily incorporated into proteins by native mammalian translation machinery, can be used to capture and identify proteins that recognize lysine PTMs, including 'readers' and 'erasers' of histone modifications.
引用
收藏
页码：70 / +
页数：6
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