期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 133, 期 43, 页码 17103-17105出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja205137d
关键词
-
资金
- National Institutes of Health [R01-AI056404, R01-AI087808]
- Welch Research Foundation [I-1561]
- Irma T. Hirschl/Monique Weill-Caulier Trust
- LERNER Trust
- NIH/NIGMS [1R01GM087544]
Protein AMPylation is an emerging post-translational modification, which plays key roles in bacterial pathogenesis and cell biology. Enzymes with AMPylation activity, referred to as AMPylators, have been identified in several bacterial pathogens and eukaryotes. To facilitate the study of this unique modification, we developed an alkynyl chemical reporter for detection and identification of protein AMPylation substrates. Covalent functionalization of AMPylation substrates with the alkynyl reporter in lieu of adenylyl 5'-monophosphate (AMP) allows their subsequent bioorthogonal ligation with azide-fluorescent dyes or affinity enrichment tags. We show that this chemical reporter is transferred by a range of AMPylators onto their cognate protein substrates and allows rapid detection and identification of AMPylated substrates.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据