Ontology highlight
ABSTRACT:
SUBMITTER: Navarro R
PROVIDER: S-EPMC4992426 | biostudies-literature | 2016 Aug
REPOSITORIES: biostudies-literature
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]