共 33 条
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.
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页码:785 / 790
页数:6
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