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

PLoS One. 2013 Aug 22;8(8):e72393. doi: 10.1371/journal.pone.0072393. eCollection 2013.

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.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Animals
  • Caenorhabditis elegans / metabolism*
  • Caenorhabditis elegans Proteins / metabolism*
  • Mice
  • NIH 3T3 Cells
  • Protein Stability*
  • Tetrahydrofolate Dehydrogenase / genetics
  • Tetrahydrofolate Dehydrogenase / metabolism

Substances

  • Caenorhabditis elegans Proteins
  • Tetrahydrofolate Dehydrogenase