A photoregulated ligand for the nuclear import receptor karyopherin alpha.
A photoregulated ligand for the nuclear import receptor karyopherin alpha.
复制标题
核输入受体核转运蛋白 α 的光调节配体。
DOI：
10.1016/s0968-0896(01)00230-9
复制
发表时间：
2001
影响因子：
3.5
通讯作者：
Standaert,RF
中科院分区：
文献类型：
--
作者：
Park,SB;Standaert,RF
协调蛋白质在细胞核和细胞质之间运输的能力为细胞提供了强大的调节机制。这些隔室之间的选择性移位通常用于传播细胞信号，并且它是控制细胞分裂、病毒复制和其他细胞事件的过程的密切部分。因此，精确的实验控制蛋白质定位，通过光的机构，将提供一个强大的工具，为研究和操纵这些事件。为此，原型光调节的核定位信号（NLS）来自于天然NLS。通过平行固相合成法制备了30个来自非洲爪蟾核质蛋白的二分NLS突变体文库，其中含有一种新的可光异构化的氨基酸，并在体外筛选其与核输入受体karyopherin α的结合，karyopherin α介导细胞蛋白质的核输入。一个单一的肽被确定，其中的顺式和反式光异构体结合的受体差异。用于获得这种肽的策略是系统的和经验的;因此，它可能适用于任何肽-受体系统。
The ability to orchestrate the transport of proteins between nucleus and cytoplasm provides cells with a powerful regulatory mechanism. Selective translocation between these compartments is often used to propagate cellular signals, and it is an intimate part of the processes that control cell division, viral replication, and other cellular events. Therefore, precise experimental control over protein localization, through the agency of light, would provide a powerful tool for the study and manipulation of these events. To this end, a prototype photoregulated nuclear localization signal (NLS) was derived from a native NLS. A library of 30 mutants of the bipartite NLS from Xenopus laevis nucleoplasmin containing a novel, photoisomerizable amino acid was prepared by parallel, solid-phase synthesis and screened in vitro for binding to the nuclear import receptor karyopherin α, which mediates the nuclear import of cellular proteins. A single peptide was identified in which the cis and trans photoisomers bind the receptor differentially. The strategy used to obtain this peptide is systematic and empirical; therefore, it is potentially applicable to any peptide-receptor system.