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Precise Control of Protein Concentration in Living Cells
Author(s) -
Lau Hubert D.,
Yaegashi Junko,
Zaro Balyn W.,
Pratt Matthew R.
Publication year - 2010
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201003073
Subject(s) - ubiquitin , complementation , chemistry , microbiology and biotechnology , protein degradation , degradation (telecommunications) , biophysics , biology , biochemistry , computer science , mutant , gene , telecommunications
Rapamycin to the rescue : Native protein concentration was precisely controlled in living cells by using the small molecule rapamycin. The addition of rapamycin “shielded” a destabilization domain from degradation and induced complementation of split ubiquitin (UbN and UbC); as a result, proteins (Pro) of interest were released. This technology enables the investigation of native protein biology over a broad concentration range.