A genetically encoded 19F NMR probe for lysine acetylation

被引：50
|
作者：
Zhang, Feng [1 ,2 ,3 ,4 ]
Zhou, Qing [2 ]
Yang, Guiwen [1 ]
An, Liguo [1 ]
Li, Fahui [2 ]
Wang, Jiangyun [2 ]
机构：
[1] Shandong Normal Univ, Coll Life Sci, Shandong Prov Key Lab Anim Resistance Biol, 88 East Wenhua Rd, Jinan 250014, Shandong, Peoples R China
[2] Chinese Acad Sci, Inst Biophys, Lab RNA Biol, 15 Datun Rd, Beijing 100101, Peoples R China
[3] Taishan Med Univ, Key Lab Atherosclerosis Univ Shandong, Tai An 271000, Shandong, Peoples R China
[4] Taishan Med Univ, Inst Atherosclerosis, Tai An 271000, Shandong, Peoples R China
来源：
CHEMICAL COMMUNICATIONS | 2018年 / 54卷 / 31期
基金：
美国国家科学基金会;
关键词：
UNNATURAL AMINO-ACIDS; HISTONE ACETYLATION; CHROMATIN-STRUCTURE; MAMMALIAN-CELLS; DNA-BINDING; POSTTRANSLATIONAL MODIFICATION; PHOTOCLICK-CHEMISTRY; PROTEIN INTERACTIONS; CROSS-LINK; P53;
D O I：
10.1039/c7cc09825a
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
Advances in acetylated protein-protein/DNA interactions depend on the development of a novel NMR (nuclear magnetic resonance) probe to study the conformational changes of acetylated proteins. However, the method for detecting the acetylated protein conformation is underdeveloped. Herein, an acetyllysine mimic has been exploited for detecting the conformational changes of acetylated p53-protein/DNA interactions by genetic code expansion and F-19 NMR. This F-19 NMR probe shows high structural similarity to acetyllysine and could not be deacetylated by sirtuin deacetylase in vitro/vivo. Moreover, acetylation of p53 K164 is reported to be deacetylated by SIRT2 for the first time.
引用
收藏
页码：3879 / 3882
页数：4
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