Importin β3 mediates the nuclear import of human ribosomal protein L7 through its interaction with the multifaceted basic clusters of L7

被引：10

作者：

Chou, Chang-Wei ^{[1
]}

Tai, Lin-Ru ^{[1
]}

Kirby, Ralph ^{[1
]}

Lee, I-Fang ^{[1
]}

Lin, Alan ^{[1
,2
]}

机构：

[1] Natl Yang Ming Univ, Inst Genome Sci, Sch Life Sci, Taipei 112, Taiwan

[2] Natl Yang Ming Univ, Inst Clin Dent Sci, Sch Dent, Taipei 112, Taiwan

来源：

FEBS LETTERS | 2010年 / 584卷 / 19期

关键词：

Eukaryotic ribosomal protein L7; Importin beta 3; Nuclear localization signal (NLS); Biosensor; Overlay assay; Fluorescence recovery after photobleaching (FRAP) assay; RIBOSOMAL-PROTEINS; LOCALIZATION; EXPRESSION; TRANSPORTIN; GENE;

D O I：

10.1016/j.febslet.2010.08.044

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We show that importin beta 3 is essential for the nuclear import of L7. The import is mediated via the multifaceted basic amino acid clusters present in the NH2-region of L7, and is RanGTP-dependent. Using a (EGFP)(3) reporter system and a FRAP assay, the role the individual clusters play as a functional NLS has been characterized, and each cluster was found to exhibit a different rate of real time nuclear uptake. We assume that having such a multiple NLS may provide L7 with preferential nuclear uptake. Structured summary: MINT-7992735: Importin beta-3 (uniprotkb: O00410) binds (MI:0407) to L7 (uniprotkb:P18124) by biophysical (MI: 0013) MINT-7992687: L7 (uniprotkb: P18124) binds (MI: 0407) to Importin beta-3 (uniprotkb: O00410) by filter binding (MI: 0049) MINT-7992699: L7 (uniprotkb: P18124) physically interacts (MI: 0915) with Importin beta-3 (uniprotkb: O00410) by affinity chromatography technology (MI: 0004) MINT-7992718: L7 (uniprotkb: P18124) physically interacts (MI: 0915) with RAN (uniprotkb:P62826) by competition binding (MI: 0405) MINT-7992671: L7 (uniprotkb: P18124) physically interacts (MI: 0915) with Importin beta-3 (uniprotkb: O00410) by pull down (MI: 0096) (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

引用

页码：4151 / 4156

页数：6

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