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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Main Authors: Ukrae Cho, Stephanie M Zimmerman, Ling-chun Chen, Elliot Owen, Jesse V Kim, Stuart K Kim, Thomas J Wandless
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2013-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC3750007?pdf=render
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author Ukrae Cho
Stephanie M Zimmerman
Ling-chun Chen
Elliot Owen
Jesse V Kim
Stuart K Kim
Thomas J Wandless
author_facet Ukrae Cho
Stephanie M Zimmerman
Ling-chun Chen
Elliot Owen
Jesse V Kim
Stuart K Kim
Thomas J Wandless
author_sort Ukrae Cho
collection DOAJ
description 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.
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spelling doaj.art-de820cb375fc4f6ba7f5eeeac877b1ef2022-12-22T02:35:54ZengPublic Library of Science (PLoS)PLoS ONE1932-62032013-01-0188e7239310.1371/journal.pone.0072393Rapid and tunable control of protein stability in Caenorhabditis elegans using a small molecule.Ukrae ChoStephanie M ZimmermanLing-chun ChenElliot OwenJesse V KimStuart K KimThomas J WandlessDestabilizing 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.http://europepmc.org/articles/PMC3750007?pdf=render
spellingShingle Ukrae Cho
Stephanie M Zimmerman
Ling-chun Chen
Elliot Owen
Jesse V Kim
Stuart K Kim
Thomas J Wandless
Rapid and tunable control of protein stability in Caenorhabditis elegans using a small molecule.
PLoS ONE
title Rapid and tunable control of protein stability in Caenorhabditis elegans using a small molecule.
title_full Rapid and tunable control of protein stability in Caenorhabditis elegans using a small molecule.
title_fullStr Rapid and tunable control of protein stability in Caenorhabditis elegans using a small molecule.
title_full_unstemmed Rapid and tunable control of protein stability in Caenorhabditis elegans using a small molecule.
title_short Rapid and tunable control of protein stability in Caenorhabditis elegans using a small molecule.
title_sort rapid and tunable control of protein stability in caenorhabditis elegans using a small molecule
url http://europepmc.org/articles/PMC3750007?pdf=render
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