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An Assay for Quantifying Protein-RNA Binding in Bacteria
Published on: June 12, 2019
Large ribosomal protein 4 increases efficiency of viral recoding sequences
Lisa Green1, Brian Houck-Loomis, Andrew Yueh
1Department of Biological Sciences, College of Physicians and Surgeons, Columbia University, New York, New York, USA.
Journal of Virology
|June 22, 2012
Summary
Large ribosomal protein 4 (RPL4) enhances viral RNA recoding efficiency, impacting viral replication. This host protein
Area of Science:
- Molecular Biology
- Virology
- Ribosome Biology
Background:
- Retroviral Pol expression necessitates translational recoding to overcome stop codons.
- Recoding occurs via stop codon readthrough or frameshift mutations.
- Host factors influencing recoding efficiency remain largely uncharacterized.
Purpose of the Study:
- To investigate the role of host protein, large ribosomal protein 4 (RPL4), in translational recoding.
- To determine the impact of RPL4 on retroviral recoding efficiency and viral particle production.
Main Methods:
- Dual luciferase reporter assays to quantify recoding efficiency.
- Transfection of cells with RPL4 cDNA and retroviral constructs.
- Analysis of viral Gag processing and particle formation.
Main Results:
- RPL4 expression dose-dependently increased recoding efficiency by up to twofold.
- RPL4 enhanced both readthrough and frameshift recoding, as well as Sindbis virus leaky termination.
- RPL4-mediated enhancement was cell line-specific and specific to RPL4 among ribosomal proteins.
Conclusions:
- RPL4 is a host factor that significantly enhances translational recoding efficiency.
- RPL4 overexpression disrupts Gag processing and reduces viral particle formation.
- RPL4's influence on the Gag-to-Gag-Pol ratio is critical for retroviral virion assembly.
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