Rapid and tunable control of protein stability in Caenorhabditis elegans using a small molecule

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...

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Bibliographic Details
Published in:PloS one 2013-08, Vol.8 (8), p.e72393-e72393
Main Authors: Cho, Ukrae, Zimmerman, Stephanie M, Chen, Ling-chun, Owen, Elliot, Kim, Jesse V, Kim, Stuart K, Wandless, Thomas J
Format: Article
Language:English
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
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Summary: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.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0072393