Nuclear import factors importin α and importin β undergo mutually induced conformational changes upon association
Nuclear import factors importin α and importin β undergo mutually induced conformational changes upon association
复制标题
DOI：
10.1016/s0014-5793(00)02154-2
复制
发表时间：
2000-11-10
期刊：
影响因子：
3.5
通讯作者：
Müller, CW
中科院分区：
文献类型：
--
作者：
Cingolani, G;Lashuel, HA;Müller, CW
输入蛋白α和输入蛋白β的异二聚体完成携带经典核定位信号（NLS）的蛋白质的核输入。这两个输入因子之间的相互作用是由输入素α的伊布结构域介导的，并涉及一个扩展的识别表面，如X射线晶体学所示。使用生物化学和生物物理技术的组合，我们已经研究了importin β：伊布结构域复合物在溶液中的形成。我们的数据表明，在结合到伊布结构域，输入蛋白β采用紧凑的，蛋白水解抗性构象，而同时伊布结构域折叠成α螺旋。我们提出了一个模型来描述这些双重相互诱导的构象变化如何可能编排核进口的NLS货物在体内。(C)2000年欧洲生物化学学会联合会。由Elsevier Science B，V.发布。保留所有权利。
A heterodimer of importin alpha and importin beta accomplishes the nuclear import of proteins carrying classical nuclear localization signals (NLS). The interaction between the two import factors is mediated by the IBB domain of importin alpha and involves an extended recognition surface as shown by X-ray crystallography. Using a combination of biochemical and biophysical techniques we have investigated the formation of the importin beta :IBB domain complex in solution. Our data suggest that upon binding to the IBB domain, importin beta adopts a compact, proteolytically resistant conformation, while simultaneously the IBB domain folds into an alpha helix. We suggest a model to describe how these dual mutually induced conformational changes may orchestrate the nuclear import of NLS cargo in vivo. (C) 2000 Federation of European Biochemical Societies. Published by Elsevier Science B,V. All rights reserved.