Recent progress with FKBP-derived destabilizing domains
Recent progress with FKBP-derived destabilizing domains
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DOI：
10.1016/j.bmcl.2008.09.043
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发表时间：
2008-11-15
影响因子：
2.7
通讯作者：
Wandless, Thomas J.
中科院分区：
文献类型：
--
作者：
Chu, Bernard W.;Banaszynski, Laura A.;Wandless, Thomas J.
fkbp衍生的不稳定结构域越来越多地被用于赋予许多不同蛋白质小分子依赖的稳定性。当L106P结构域融合到n端、c端或剪接到黄色荧光蛋白中间时，它赋予黄色荧光蛋白不稳定性，但L106P的多个拷贝不会赋予更大的不稳定性。这些工程的不稳定结构域在调节蛋白质稳定性的内源性降解中并不占主导地位。(C) 2008 Elsevier Ltd版权所有。
The FKBP-derived destabilizing domains are increasingly being used to confer small molecule-dependent stability to many different proteins. The L106P domain confers instability to yellow fluorescent protein when it is fused to the N-terminus, the C-terminus, or spliced into the middle of yellow fluorescent protein, however multiple copies of L106P do not confer greater instability. These engineered destabilizing domains are not dominant to endogenous degrons that regulate protein stability. (C) 2008 Elsevier Ltd. All rights reserved.