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Mouse p56 blocks a distinct function of eukaryotic initiation factor 3 in translation initiation
Daniel J Hui1, Fulvia Terenzi, William C Merrick
1Department of Molecular Biology, The Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, Ohio 44195, USA.
The Journal of Biological Chemistry
|November 25, 2004
Summary
Mouse and human p56 proteins inhibit translation by targeting eukaryotic initiation factor 3 (eIF3). However, they bind to different eIF3 subunits, blocking distinct steps in translation initiation.
Area of Science:
- Molecular Biology
- Virology
- Biochemistry
Background:
- Mammalian p56 proteins are induced by viral infections and interferons.
- Human p56 inhibits translation by binding the eukaryotic initiation factor 3 (eIF3)
- e
- subunit, disrupting the ternary complex interaction.
Purpose of the Study:
- To investigate the mechanism of mouse p56 in translation inhibition.
- To compare the interaction of mouse p56 with human p56 and eukaryotic initiation factor 3 (eIF3).
Main Methods:
- Protein-protein interaction studies.
- Translation inhibition assays.
- Analysis of eukaryotic initiation factor 3 (eIF3) subunit binding.
Main Results:
- Mouse p56 inhibits translation by binding to the "c" subunit of eukaryotic initiation factor 3 (eIF3).
- Mouse p56 binding to eIF3 has a marginal effect on the ternary complex interaction.
- Mouse p56 primarily inhibits the binding of eIF4F to the 40S ribosomal subunit.
Conclusions:
- Mouse and human p56 proteins exhibit distinct mechanisms for inhibiting translation.
- The differential binding of p56 proteins to eukaryotic initiation factor 3 (eIF3) subunits underlies their varied inhibitory effects on translation initiation.