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A Novel Destabilizing Domain Based on a Small-Molecule Dependent Fluorophore.


ABSTRACT: 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.

SUBMITTER: Navarro R 

PROVIDER: S-EPMC4992426 | biostudies-literature | 2016 Aug

REPOSITORIES: biostudies-literature

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A Novel Destabilizing Domain Based on a Small-Molecule Dependent Fluorophore.

Navarro Raul R   Chen Ling-Chun LC   Rakhit Rishi R   Wandless Thomas J TJ  

ACS chemical biology 20160606 8


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 degradat  ...[more]

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