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Published on: October 15, 2019
Cellular coexistence of two high molecular subsets of eEF1B complex
Frédéric Le Sourd1, Patrick Cormier, Stéphane Bach
1Equipe Cycle Cellulaire et Développement, Unité Mixte de Recherche Mer & Santé, UMR 7150, Centre National de la Recherche Scientifique, CNRS, Université Pierre et Marie Curie, UPMC, Station Biologique de Roscoff, 29682 Roscoff, Cedex, France.
FEBS Letters
|May 2, 2006
Summary
Two isoforms of the elongation factor eEF1Bdelta were identified in sea urchin eggs, differing by a 26-amino acid insert. These isoforms are co-expressed and form distinct protein complexes, suggesting a novel regulatory mechanism in protein translation.
Area of Science:
- Molecular Biology
- Cell Biology
- Protein Synthesis
Background:
- The elongation factor eEF1B plays a crucial role in protein translation.
- Understanding the diversity and function of its subunits is essential for comprehending translational regulation.
Purpose of the Study:
- To investigate the isoforms of the eEF1Bdelta subunit in sea urchin eggs.
- To determine the co-expression and complex formation of these isoforms.
Main Methods:
- In silico analysis of EST databases for metazoan homologs.
- Co-immunoprecipitation using specific eEF1Bdelta2 antibodies.
- Quantitative immunoblotting to assess protein levels in complexes.
Main Results:
- Identified two eEF1Bdelta isoforms (eEF1Bdelta1 and eEF1Bdelta2) in sea urchin eggs, with eEF1Bdelta2 containing a 26-amino acid insert.
- Both isoforms are co-expressed and likely derived from a single gene.
- Demonstrated that eEF1Bdelta1 and eEF1Bdelta2 proteins exist in distinct subsets of the eEF1B complex.
Conclusions:
- The presence of two distinct eEF1Bdelta isoforms suggests a specialized role in translational control.
- A model for the differential assembly of eEF1B complexes is proposed.
- The observed phenomenon appears conserved across metazoans.
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