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

39Citations
Citations of this article
97Readers
Mendeley users who have this article in their library.

Abstract

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. © 2013 Cho et al.

Cite

CITATION STYLE

APA

Cho, U., Zimmerman, S. M., Chen, L. chun, Owen, E., Kim, J. V., Kim, S. K., & Wandless, T. J. (2013). Rapid and Tunable Control of Protein Stability in Caenorhabditis elegans Using a Small Molecule. PLoS ONE, 8(8). https://doi.org/10.1371/journal.pone.0072393

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free