期刊
CHEMBIOCHEM
卷 16, 期 18, 页码 2605-2609出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.201500427
关键词
bioorthogonal chemical probes; click reaction; FRET; HAT activity; protein acetylation
资金
- NSF [1507741]
- AHA [12GRNT12070056]
- NIH [R01M086717]
- China Scholarship Council
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [1507741] Funding Source: National Science Foundation
Histone acetyltransferases (HATs) are key players in the epigenetic regulation of gene function. The recent discovery of diverse HAT substrates implies a broad spectrum of cellular functions of HATs. Many pathological processes are also intimately associated with the dysregulation of HAT levels and activities. However, detecting the enzymatic activity of HATs has been challenging, and this has significantly impeded drug discovery. To advance the field, we developed a convenient one-pot, mix-and-read strategy that is capable of directly detecting the acylated histone product through a fluorescent readout. The strategy integrates three technological platforms-bioorthogonal HAT substrate labeling, alkyne-azide click chemistry, and quenching FRET-into one system for effective probing of HAT enzyme activity.
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