ArticleNucleic acids research2009
Translation of intronless RNAs is strongly stimulated by the Epstein-Barr virus mRNA export factor EB2.
Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 31 citations in OpenAlex.
- Review
- The double-stranded RNA-binding protein, Staufen1, is an IRES-transacting factor regulating HIV-1 cap-independent translation initiation.Nucleic acids research · 2022Article
- The Epstein-Barr Virus Lytic Protein BMLF1 Induces Upregulation of GRP78 Expression through ATF6 Activation.International journal of molecular sciences · 2021Article
- Post-translational modifications of hnRNP A1 differentially modulate retroviral IRES-mediated translation initiation.Nucleic acids research · 2020Article
- Cellular RNA Helicase DHX9 Interacts with the Essential Epstein-Barr Virus (EBV) Protein SM and Restricts EBV Lytic Replication.Journal of virology · 2019Article
- Epstein-Barr Virus-Induced Nodules on Viral Replication Compartments Contain RNA Processing Proteins and a Viral Long Noncoding RNA.Journal of virology · 2018Article
- The splicing factor SRSF3 is functionally connected to the nuclear RNA exosome for intronless mRNA decay.Scientific reports · 2018Article
- Efficient Translation of Epstein-Barr Virus (EBV) DNA Polymerase Contributes to the Enhanced Lytic Replication Phenotype of M81 EBV.Journal of virology · 2018Article
- Epstein-Barr Virus Protein EB2 Stimulates Translation Initiation of mRNAs through Direct Interactions with both Poly(A)-Binding Protein and Eukaryotic Initiation Factor 4G.Journal of virology · 2018Article
- KSHV inhibits stress granule formation by viral ORF57 blocking PKR activation.PLoS pathogens · 2017Article
- Modulation of the Translational Landscape During Herpesvirus Infection.Annual review of virology · 2015Review
- HIV-2 genomic RNA accumulates in stress granules in the absence of active translation.Nucleic acids research · 2014Article
- Epstein-Barr virus nuclear antigen 3A protein regulates CDKN2B transcription via interaction with MIZ-1.Nucleic acids research · 2014Article
- Staufen1 senses overall transcript secondary structure to regulate translation.Nature structural & molecular biology · 2014Article
- Epstein-Barr virus protein EB2 stimulates cytoplasmic mRNA accumulation by counteracting the deleterious effects of SRp20 on viral mRNAs.Nucleic acids research · 2012Article
- Different effects of the TAR structure on HIV-1 and HIV-2 genomic RNA translation.Nucleic acids research · 2012Article
- The Andes hantavirus NSs protein is expressed from the viral small mRNA by a leaky scanning mechanism.Journal of virology · 2012Article
- The Kaposi's Sarcoma-Associated Herpesvirus ORF57 Protein and Its Multiple Roles in mRNA Biogenesis.Frontiers in microbiology · 2012Article
- Activation of a microRNA response in trans reveals a new role for poly(A) in translational repression.Nucleic acids research · 2011Article
- The 3' untranslated region of the Andes hantavirus small mRNA functionally replaces the poly(A) tail and stimulates cap-dependent translation initiation from the viral mRNA.Journal of virology · 2010Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Epstein-Barr virus protein (EB2) allows the nuclear export of a particular subset of early and late viral RNAs derived from intronless genes. EB2 is conserved among most herpesvirus members and its presence is essential for the production of infectious particles. Here we show that, besides its role as a nuclear export factor, EB2 strongly stimulates translation of unspliced mRNAs without affecting overall cellular translation. Interestingly, this effect can be reversed by the addition of an intron within the gene. The spliced mRNA is then efficiently exported and translated even in the absence of EB2. Moreover, we show that EB2 associates with translating ribosomes and increases the proportion of its target RNA in the polyribosomal fraction. Finally, testing of EB2 homolog proteins derived from EBV-related herpesviruses, shows that, even if they play similar roles within the replication cycle of their respective virus, their mechanisms of action are different.
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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.