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
相关论文
共 33 条
[1]   TRANSLATION IN SACCHAROMYCES-CEREVISIAE - INITIATION-FACTOR 4E-DEPENDENT CELL-FREE SYSTEM [J].
ALTMANN, M ;
SONENBERG, N ;
TRACHSEL, H .
MOLECULAR AND CELLULAR BIOLOGY, 1989, 9 (10) :4467-4472
[2]   Functional interactions between yeast translation eukaryotic elongation factor (eEF) 1A and eEF3 [J].
Anand, M ;
Chakraburtty, K ;
Marton, MJ ;
Hinnebusch, AG ;
Kinzy, TG .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (09) :6985-6991
[3]  
[Anonymous], 1991, Methods Enzymol, V194, P1
[4]   Interactions of elongation factor EF-P with the Escherichia coli ribosome [J].
Aoki, Hiroyuki ;
Xu, John ;
Emili, Andrew ;
Chosay, John G. ;
Golshani, Ashkan ;
Ganoza, M. Clelia .
FEBS JOURNAL, 2008, 275 (04) :671-681
[5]  
BENNE R, 1978, J BIOL CHEM, V253, P3078
[6]  
Chen KY, 1997, BIOL SIGNAL, V6, P105
[7]   General translational repression by activators of mRNA decapping [J].
Coller, J ;
Parker, R .
CELL, 2005, 122 (06) :875-886
[8]   Structural modeling and mutational analysis of yeast eukaryotic translation initiation factor 5A reveal new critical residues and reinforce its involvement in protein synthesis [J].
Dias, Camila A. O. ;
Cano, Veridiana S. P. ;
Rangel, Suzana M. ;
Apponi, Luciano H. ;
Frigieri, Mariana C. ;
Muniz, Joao R. C. ;
Garcia, Wanius ;
Park, Myung H. ;
Garratt, Richard C. ;
Zanelli, Cleslei F. ;
Valentini, Sandro R. .
FEBS JOURNAL, 2008, 275 (08) :1874-1888
[9]   REGULATION OF PROTEIN SYNTHESIS IN MAMMALIAN CELLS .2. INHIBITION OF PROTEIN SYNTHESIS AT LEVEL OF INITIATION DURING MITOSIS [J].
FAN, H ;
PENMAN, S .
JOURNAL OF MOLECULAR BIOLOGY, 1970, 50 (03) :655-&
[10]  
Frigieri MC, 2007, GENET MOL RES, V6, P152