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鉴定hSRP1α作为核定位序列的功能性受体。

Identification of hSRP1 alpha as a functional receptor for nuclear localization sequences.

作者信息

Weis K, Mattaj I W, Lamond A I

机构信息

European Molecular Biology Laboratory, Heidelberg, Germany.

出版信息

Science. 1995 May 19;268(5213):1049-53. doi: 10.1126/science.7754385.

DOI:10.1126/science.7754385
PMID:7754385
Abstract

Import of proteins into the nucleus is a two-step process, involving nuclear localization sequence (NLS)-dependent docking of the substrate at the nuclear envelope followed by translocation through the nuclear pore. A recombinant human protein, hSRP1 alpha, bound in vitro specifically and directly to substrates containing either a simple or bipartite NLS motif. hSRP1 alpha promoted docking of import substrates to the nuclear envelope and together with recombinant human Ran reconstituted complete nuclear protein import. Thus, hSRP1 alpha has the properties of a cytosolic receptor for both simple and bipartite NLS motifs.

摘要

蛋白质进入细胞核是一个两步过程,包括底物在核膜上依赖核定位序列(NLS)的对接,随后通过核孔进行转运。一种重组人蛋白hSRP1α,在体外能特异性且直接地与含有简单或双分NLS基序的底物结合。hSRP1α促进输入底物与核膜的对接,并与重组人Ran一起重建了完整的核蛋白输入过程。因此,hSRP1α具有作为简单和双分NLS基序的胞质受体的特性。

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