期刊
ACS CHEMICAL BIOLOGY
卷 11, 期 8, 页码 2101-2104出版社
AMER CHEMICAL SOC
DOI: 10.1021/acschembio.6b00234
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资金
- National Institutes of Health [GM073046]
- National Science Foundation [1306670]
- Canadian Institutes of Health Research
- Stanford Shared FACS Facility (NIH Shared Instrumentation Grant) [SS10RR027431]
- Direct For Biological Sciences
- Div Of Biological Infrastructure [1306670] Funding Source: National Science Foundation
Tools that can directly regulate the activity of any protein-of-interest are valuable in the study of complex biological processes. Herein, we describe the development of a novel protein domain that exhibits small molecule-dependent stability and fluorescence based on the bilirubin-inducible fluorescent protein, UnaG. When genetically fused to any protein-of-interest, this fluorescent destabilizing domain (FDD) confers its instability to the entire fusion protein, facilitating the rapid degradation of the fusion. In the presence of its cognate ligand bilirubin (BR), the FDD fusion becomes stable and fluorescent. This new chemical genetic tool allows for rapid, reversible, and tunable control over the stability and fluorescence of a wide range of protein targets.
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