Document Detail

Translation of Sindbis virus 26S mRNA does not require intact eukariotic initiation factor 4G.
MedLine Citation:
PMID:  16343528     Owner:  NLM     Status:  MEDLINE    
The infection of baby hamster kidney (BHK) cells by Sindbis virus gives rise to a drastic inhibition of cellular translation, while under these conditions the synthesis of viral structural proteins directed by the subgenomic 26S mRNA takes place efficiently. Here, the requirement for intact initiation factor eIF4G for the translation of this subgenomic mRNA has been examined. To this end, SV replicons that contain the protease of human immunodeficiency virus type 1 (HIV-1) or the poliovirus 2A(pro) replacing the sequences of SV glycoproteins have been constructed. BHK cells electroporated with the different RNAs synthesize protein C and the corresponding protease at late times. Notably, the proteolysis of eIF4G by both proteases has little effect on the translation of the 26S mRNA. In addition, recombinant viable SVs were engineered that encode HIV-1 PR or poliovirus 2A protease under the control of a duplicated late promoter. Viral protein synthesis at late times of infection by the recombinant viruses is slightly affected in BHK cells that contain proteolysed eIF4G. The translatability of SV genomic 49S mRNA was assayed in BHK cells infected with a recombinant virus that synthesizes luciferase and transfected with a replicon that expresses poliovirus 2Apro. Under conditions where eIF4G has been hydrolysed significantly the translation of genomic SV RNA was deeply inhibited. These findings indicate a different requirement for intact eIF4G in the translation of genomic and subgenomic SV mRNAs. Finally, the translation of the reporter gene that encodes green fluorescent protein, placed under the control of a second duplicate late promoter, is also resistant to the cleavage of eIF4G. In conclusion, despite the presence of a cap structure in the 5' end of the subgenomic SV mRNA, intact eIF4G is not necessary for its translation.
Alfredo Castelló; Miguel Angel Sanz; Susana Molina; Luis Carrasco
Related Documents :
1875198 - Expression strategy of the potato virus x triple gene block.
18928538 - Ectopic expression of a truncated cd40l protein from synthetic post-transcriptionally c...
25394548 - Heme-binding-mediated negative regulation of the tryptophan metabolic enzyme indoleamin...
7989338 - Translational control mediates the developmental regulation of the trypanosoma brucei n...
7706718 - Human placental hla-g expression is restricted to differentiated cytotrophoblasts.
16317718 - Caenorhabditis elegans expresses three functional profilins in a tissue-specific manner.
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2005-11-28
Journal Detail:
Title:  Journal of molecular biology     Volume:  355     ISSN:  0022-2836     ISO Abbreviation:  J. Mol. Biol.     Publication Date:  2006 Feb 
Date Detail:
Created Date:  2006-01-02     Completed Date:  2006-03-14     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985088R     Medline TA:  J Mol Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  942-56     Citation Subset:  IM    
Centro de Biología Molecular "Severo Ochoa" (CSIC-UAM), Facultad de Ciencias, Universidad Autónoma de Madrid, Cantoblanco, 28049 Madrid, Spain.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Cell Line
Eukaryotic Initiation Factor-4G / metabolism*
HIV-1 / genetics
Poliovirus / genetics
Protein Biosynthesis*
RNA, Messenger / genetics,  metabolism*
RNA, Viral*
Recombinant Fusion Proteins* / genetics,  metabolism
Sindbis Virus / genetics,  metabolism
Reg. No./Substance:
0/Eukaryotic Initiation Factor-4G; 0/RNA, Messenger; 0/RNA, Viral; 0/Recombinant Fusion Proteins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Protein translocation through the anthrax toxin transmembrane pore is driven by a proton gradient.
Next Document:  Quantitative analysis of deoxynucleotide substitutions in the codon-anticodon helix.