eIF5A binds to translational machinery components and affects translation in yeast

被引：88

作者：

Zanelli, Cleslei F.

Maragno, Ana L. C.

Gregio, Ana P. B.

Komili, Suzanne

Pandolfi, Jose R.

Mestriner, Carlos A.

Lustri, Wilton R.

Valentini, Sandro R. ^{[1
]}

机构：

[1] UNESP, Sch Pharmaceut Sci, Dept Biol Sci, BR-14801902 Araraquara, SP, Brazil

[2] Harvard Univ, Sch Med, Dept Syst Biol, Boston, MA 02115 USA

[3] Harvard Univ, Sch Med, Dept Biol Chem & Mol Pharmacol, Boston, MA 02115 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2006年 / 348卷 / 04期

基金：

巴西圣保罗研究基金会;

关键词：

eIF5A; ribosome; translation; eEF2; P0; L11; hypusine; protein synthesis;

D O I：

10.1016/j.bbrc.2006.07.195

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：

The putative translation factor eIF5A is essential for cell viability and is highly conserved from archebacteria to mammals. Although this protein was originally identified as a translation initiation factor, subsequent experiments did not support a role for eIF5A in general translation. In this work, we demonstrate that eIF-5A interacts with structural components of the 80S ribosome, as well as with the translation elongation factor 2 (eEF2). Moreover, eIF5A is further shown to cofractionate with monosomes in a translation-dependent manner. Finally, eIF5A mutants show altered polysome profiles and are sensitive to translation inhibitors. Our results re-establish a function for eIF5A in translation and suggest a role for this factor in translation elongation instead of translation initiation. (c) 2006 Elsevier Inc. All rights reserved.

引用

页码：1358 / 1366

页数：9

共 55 条

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