eIF5A has a function in the elongation step of translation in yeast

被引:103
作者
Gregio, Ana P. B. [1 ]
Cano, Veridiana P. S. [1 ]
Avaca, Juliana S. [1 ]
Valentini, Sandro R. [1 ]
Zanelli, Cleslei F. [1 ]
机构
[1] Sao Paulo State Univ, Dept Biol Sci, Sch Pharmaceut Sci, UNESP,Fac Ciencias Farmaceut, BR-14801902 Araraquara, SP, Brazil
基金
巴西圣保罗研究基金会;
关键词
eIF5A; Translation elongation; eEF2; Ribosome transit time; EF-P; Hypusine; INITIATION-FACTOR; 5A; SACCHAROMYCES-CEREVISIAE; PROTEIN-SYNTHESIS; MESSENGER-RNAS; HYPUSINE MODIFICATION; STABILIZATION; INHIBITION; REVEAL; BODIES; MUTANT;
D O I
10.1016/j.bbrc.2009.01.148
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 throughout evolution. Here, we describe genetic interactions between an eIF5A Mutant and a translation initiation mutant (eIF4E) or a translation elongation mutant (eEF2). Polysome profile analysis of single and double mutants revealed that mutation in eIF5A reduces polysome run-off, contrarily to translation initiation mutants. Moreover, the polysome profile of an eIF5A mutant alone is very similar to that of a translation elongation mutant. Furthermore, depletion of eIF5A causes a significant decrease in total protein synthesis and an increase of the average ribosome transit time. Finally, we, demonstrate that the formation of P bodies is inhibited in an eIF5A mutant, similarly to the effect of the translation elongation inhibitor cycloheximide. taken together, these results not only reinforce a role for eIF5A in translation but also strongly support a function for eIF5A in the elongation step of protein synthesis. (C) 2009 Elsevier Inc. All rights reserved.
引用
收藏
页码:785 / 790
页数:6
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