Rapid and Tunable Control of Protein Stability in Caenorhabditis elegans Using a Small Molecule

• Published in: PloS one Vol. 8; no. 8; p. e72393
• Main Authors: Cho, Ukrae, Zimmerman, Stephanie M., Chen, Ling-chun, Owen, Elliot, Kim, Jesse V., Kim, Stuart K., Wandless, Thomas J.
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 22.08.2013; Public Library of Science (PLoS)
• Subjects: Animals; Biology; Caenorhabditis elegans; Caenorhabditis elegans - metabolism; Caenorhabditis elegans Proteins - metabolism; Chemistry; Control stability; Developmental biology; Dihydrofolate reductase; Experiments; Fusion protein; Gene expression; Ligands; Mice; Nematodes; NIH 3T3 Cells; Physics; Protein expression; Protein Stability; Proteins; Studies; Technology; Temperature; Tetrahydrofolate Dehydrogenase - genetics; Tetrahydrofolate Dehydrogenase - metabolism; Worms; United States > US; California
• ISSN: 1932-6203; 1932-6203
• DOI: 10.1371/journal.pone.0072393

Destabilizing domains are conditionally unstable protein domains that can be fused to a protein of interest resulting in degradation of the fusion protein in the absence of stabilizing ligand. These engineered protein domains enable rapid, reversible and dose-dependent control of protein expression levels in cultured cells and in vivo. To broaden the scope of this technology, we have engineered new destabilizing domains that perform well at temperatures of 20-25°C. This raises the possibility that our technology could be adapted for use at any temperature. We further show that these new destabilizing domains can be used to regulate protein concentrations in C. elegans. These data reinforce that DD can function in virtually any organism and temperature.