scholarly journals Iron Regulates Hepatitis C Virus Translation via Stimulation of Expression of Translation Initiation Factor 3

2004 ◽  
Vol 190 (4) ◽  
pp. 819-825 ◽  
Author(s):  
Igor Theurl ◽  
Heinz Zoller ◽  
Peter Obrist ◽  
Christian Datz ◽  
Felix Bachmann ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Translation Initiation ◽  
Translation Initiation Factor ◽  
Initiation Factor ◽  
Translation Initiation Factor 3 ◽  
Stimulation Of

Structure of a hepatitis C virus IRES RNA motif recognized by translation initiation factor 3

2002 ◽  
Vol 30 (1) ◽  
pp. A18-A18
Author(s):  
José Gallego ◽  
Roscoe Klinck ◽  
A. Collier ◽  
G. Harrison ◽  
S. Harris ◽  
...  
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Translation Initiation ◽  
Translation Initiation Factor ◽  
Initiation Factor ◽  
Rna Motif ◽  
Translation Initiation Factor 3

scholarly journals Control of Paip1-Eukayrotic Translation Initiation Factor 3 Interaction by Amino Acids through S6 Kinase

2014 ◽  
Vol 34 (6) ◽  
pp. 1046-1053 ◽  
Author(s):  
Y. Martineau ◽  
X. Wang ◽  
T. Alain ◽  
E. Petroulakis ◽  
D. Shahbazian ◽  
...  
Keyword(s):  
Amino Acids ◽  
Translation Initiation ◽  
Translation Initiation Factor ◽  
Initiation Factor ◽  
S6 Kinase ◽  
Translation Initiation Factor 3

scholarly journals Translation initiation by the hepatitis C virus IRES requires eIF1A and ribosomal complex remodeling

eLife ◽  
2016 ◽  
Vol 5 ◽  
Author(s):  
Zane A Jaafar ◽  
Akihiro Oguro ◽  
Yoshikazu Nakamura ◽  
Jeffrey S Kieft
Keyword(s):  
Hepatitis C Virus ◽  
Hepatitis C ◽  
Translation Initiation ◽  
Rna Structure ◽  
Initiation Factor ◽  
Internal Ribosome Entry ◽  
Eukaryotic Translation ◽  
Eukaryotic Translation Initiation ◽  
Hcv Ires ◽  
Type 3

Internal ribosome entry sites (IRESs) are important RNA-based translation initiation signals, critical for infection by many pathogenic viruses. The hepatitis C virus (HCV) IRES is the prototype for the type 3 IRESs and is also invaluable for exploring principles of eukaryotic translation initiation, in general. Current mechanistic models for the type 3 IRESs are useful but they also present paradoxes, including how they can function both with and without eukaryotic initiation factor (eIF) 2. We discovered that eIF1A is necessary for efficient activity where it stabilizes tRNA binding and inspects the codon-anticodon interaction, especially important in the IRES’ eIF2-independent mode. These data support a model in which the IRES binds preassembled translation preinitiation complexes and remodels them to generate eukaryotic initiation complexes with bacterial-like features. This model explains previous data, reconciles eIF2-dependent and -independent pathways, and illustrates how RNA structure-based control can respond to changing cellular conditions.

scholarly journals Binding of eukaryotic translation initiation factor 4E (eIF4E) to eIF4G represses translation of uncapped mRNA.

1997 ◽  
Vol 17 (12) ◽  
pp. 6876-6886 ◽  
Author(s):  
S Z Tarun ◽  
A B Sachs
Keyword(s):  
Translation Initiation ◽  
Mrna Translation ◽  
Translation Initiation Factor ◽  
Initiation Factor ◽  
Eukaryotic Translation Initiation Factor ◽  
Eukaryotic Translation ◽  
Eukaryotic Translation Initiation ◽  
Stimulation Of

mRNA translation in crude extracts from the yeast Saccharomyces cerevisiae is stimulated by the cap structure and the poly(A) tail through the binding of the cap-binding protein eukaryotic translation initiation factor 4E (eIF4E) and the poly(A) tail-binding protein Pab1p. These proteins also bind to the translation initiation factor eIF4G and thereby link the mRNA to the general translational apparatus. In contrast, uncapped, poly(A)-deficient mRNA is translated poorly in yeast extracts, in part because of the absence of eIF4E and Pab1p binding sites on the mRNA. Here, we report that uncapped-mRNA translation is also repressed in yeast extracts due to the binding of eIF4E to eIF4G. Specifically, we find that mutations which weaken the eIF4E binding site on the yeast eIF4G proteins Tif4631p and Tif4632p lead to temperature-sensitive growth in vivo and the stimulation of uncapped-mRNA translation in vitro. A mutation in eIF4E which disturbs its ability to interact with eIF4G also leads to a stimulation of uncapped-mRNA translation in vitro. Finally, overexpression of eIF4E in vivo or the addition of excess eIF4E in vitro reverses these effects of the mutations. These data support the hypothesis that the eIF4G protein can efficiently stimulate translation of exogenous uncapped mRNA in extracts but is prevented from doing so as a result of its association with eIF4E. They also suggest that some mRNAs may be translationally regulated in vivo in response to the amount of free eIF4G in the cell.

Sign in / Sign up

Export Citation Format

Share Document