ArticleThe EMBO journal2001
Truncated initiation factor eIF4G lacking an eIF4E binding site can support capped mRNA translation.
Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed, 79 citations in OpenAlex.
- Mechanisms and consequences of mRNA destabilization during viral infections.Virology journal · 2024Review
- The SARS-unique domain (SUD) of SARS-CoV and SARS-CoV-2 interacts with human Paip1 to enhance viral RNA translation.The EMBO journal · 2021Article
- eIF4G-driven translation initiation of downstream ORFs in mammalian cells.Nucleic acids research · 2020Article
- Toward a Kinetic Understanding of Eukaryotic Translation.Cold Spring Harbor perspectives in biology · 2019Review
- Parkinson Disease from Mendelian Forms to Genetic Susceptibility: New Molecular Insights into the Neurodegeneration Process.Cellular and molecular neurobiology · 2018Review
- Concerted action of two 3' cap-independent translation enhancers increases the competitive strength of translated viral genomes.Nucleic acids research · 2017Article
- eIF4E binding protein 1 expression is associated with clinical survival outcomes in colorectal cancer.Oncotarget · 2015Article
- Role of translation initiation factor 4G in lifespan regulation and age-related health.Ageing research reviews · 2014Review
- 40S recruitment in the absence of eIF4G/4A by EMCV IRES refines the model for translation initiation on the archetype of Type II IRESs.Nucleic acids research · 2014Article
- Role of RNA structure motifs in IRES-dependent translation initiation of the coxsackievirus B3: new insights for developing live-attenuated strains for vaccines and gene therapy.Molecular biotechnology · 2013Review
- In vitro molecular characterization of RNA-proteins interactions during initiation of translation of a wild-type and a mutant Coxsackievirus B3 RNAs.Molecular biotechnology · 2013Article
- A novel mechanism of eukaryotic translation initiation that is neither m7G-cap-, nor IRES-dependent.Nucleic acids research · 2013Article
- DNA damage and eIF4G1 in breast cancer cells reprogram translation for survival and DNA repair mRNAs.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Translation directed by hepatitis A virus IRES in the absence of active eIF4F complex and eIF2.PloS one · 2012Article
- Further characterisation of the translational termination-reinitiation signal of the influenza B virus segment 7 RNA.PloS one · 2011Article
- Reversing chemoresistance by small molecule inhibition of the translation initiation complex eIF4F.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Time-dependent increase in ribosome processivity.Nucleic acids research · 2010Article
- The 5'-7-methylguanosine cap on eukaryotic mRNAs serves both to stimulate canonical translation initiation and to block an alternative pathway.Molecular cell · 2010Article
- Mechanism of initiation site selection promoted by the human rhinovirus 2 internal ribosome entry site.Journal of virology · 2010Article
- A protein that replaces the entire cellular eIF4F complex.The EMBO journal · 2008Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Picornavirus proteases cleave translation initiation factor eIF4G into a C-terminal two-thirds fragment (hereafter named p100) and an N-terminal one-third fragment, which interacts with the cap-binding factor eIF4E. As the timing of this cleavage correlates broadly with the shut-off of host cell protein synthesis in infected cells, a very widespread presumption has been that p100 cannot support capped mRNA translation. Through the use of an eIF4G-depleted reticulocyte lysate system, we show that this presumption is incorrect. Moreover, recombinant p100 can also reverse the inhibition of capped mRNA translation caused either by m7GpppG cap analogue, by 4E-BP1, which sequesters eIF4E and thus blocks its association with eIF4G, or by cleavage of endogenous eIF4G by picornavirus proteases. The concentration of p100 required for maximum translation of capped mRNAs is approximately 4-fold higher than the endogenous eIF4G concentration in reticulocyte lysates. Our results imply that picornavirus-induced shut-off is not due to an intrinsic inability of p100 to support capped mRNA translation, but to the viral RNA outcompeting host cell mRNA for the limiting concentration of p100.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.