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...
Main Authors: | , , , , , , |
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Format: | Article |
Language: | English |
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Public Library of Science (PLoS)
2013-01-01
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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. |
first_indexed | 2024-04-13T18:10:41Z |
format | Article |
id | doaj.art-de820cb375fc4f6ba7f5eeeac877b1ef |
institution | Directory Open Access Journal |
issn | 1932-6203 |
language | English |
last_indexed | 2024-04-13T18:10:41Z |
publishDate | 2013-01-01 |
publisher | Public Library of Science (PLoS) |
record_format | Article |
series | PLoS ONE |
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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