mRNA decay during herpesvirus infections: interaction between a putative viral nuclease and a cellular translation factor
| Autor: | G. Sullivan Read, David N. Everly, Pinghui Feng |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
Immunoprecipitation
Immunology Molecular Sequence Data RNA-binding protein Biology medicine.disease_cause Microbiology Viral Proteins Eukaryotic translation Ribonucleases Peptide Initiation Factors Virology Eukaryotic initiation factor Gene expression Chlorocebus aethiops medicine Animals Simplexvirus Translation factor Amino Acid Sequence RNA Messenger Eukaryotic Initiation Factors Vero Cells Binding Sites RNA-Binding Proteins Molecular biology Virus-Cell Interactions Herpes simplex virus Lytic cycle Insect Science |
| Zdroj: | Journal of virology. 75(21) |
| ISSN: | 0022-538X |
| Popis: | During lytic infections, the virion host shutoff (Vhs) protein (UL41) of herpes simplex virus destabilizes both host and viral mRNAs. By accelerating mRNA decay, it helps determine the levels and kinetics of viral and cellular gene expression. In vivo, Vhs shows a strong preference for mRNAs, as opposed to non-mRNAs, and degrades the 5′ end of mRNAs prior to the 3′ end. In contrast, partially purified Vhs is not restricted to mRNAs and causes cleavage of target RNAs at various sites throughout the molecule. To explain this discrepancy, we searched for cellular proteins that interact with Vhs using the Saccharomyces cerevisiae two-hybrid system. Vhs was found to interact with the human translation initiation factor, eIF4H. This interaction was verified by glutathione S -transferase pull-down experiments and by coimmunoprecipitation of Vhs and epitope-tagged eIF4H from extracts of mammalian cells. The interaction was abolished by several point mutations in Vhs that abrogate its ability to degrade mRNAs in vivo. The results suggest that Vhs is a viral mRNA degradation factor that is targeted to mRNAs, and to regions of translation initiation, through an interaction with eIF4H. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|