Rapid and Tunable Control of Protein Stability in Caenorhabditis elegans Using a Small Molecule
Rapid and Tunable Control of Protein Stability in Caenorhabditis elegans Using a Small Molecule
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DOI：
10.1371/journal.pone.0072393
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发表时间：
2013-08-22
期刊：
影响因子：
3.7
通讯作者：
Wandless, Thomas J.
中科院分区：
文献类型：
--
作者：
Cho, Ukrae;Zimmerman, Stephanie M.;Wandless, Thomas J.
去稳定化结构域是条件不稳定的蛋白质结构域，其可以与目的蛋白质融合，导致融合蛋白在不存在稳定化配体的情况下降解。这些工程化的蛋白质结构域能够快速、可逆和剂量依赖性地控制培养细胞和体内的蛋白质表达水平。为了扩大这项技术的应用范围，我们设计了新的去稳定域，在20-25摄氏度的温度下表现良好。这增加了我们的技术可以在任何温度下使用的可能性。我们进一步表明，这些新的去稳定结构域可用于调节C.优美的这些数据进一步证实，DD几乎可以在任何生物体和温度下发挥作用。
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 degrees 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.