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Updated: Jun 5, 2026
08:47
Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells
Published on: May 1, 2020
The translational repressor 4E-BP called to order by eIF4E: new structural insights by SAXS
Pauline Gosselin1, Nathalie Oulhen, Murielle Jam
1UPMC Univ Paris 06, UMR 7150, Mer et Santé, Equipe Traduction Cycle Cellulaire et Développement, Station Biologique de Roscoff, 29680 Roscoff, France. gosselin@sb-roscoff.fr
Nucleic Acids Research
|December 25, 2010
Summary
The eIF4E binding protein (4E-BP) is intrinsically disordered but compacts upon binding to eIF4E. This forms a
Area of Science:
- Molecular Biology
- Structural Biology
- Biochemistry
Background:
- eIF4E binding protein (4E-BP) regulates mRNA translation by interacting with the initiation factor eIF4E.
- 4E-BP is generally considered unstructured in both free and bound states, influencing translation inhibition.
Purpose of the Study:
- To investigate the structural dynamics of 4E-BP in solution.
- To elucidate the structural changes of 4E-BP upon binding to eIF4E.
- To characterize the nature of the eIF4E/4E-BP complex.
Main Methods:
- Small-angle X-ray scattering (SAXS) was employed to analyze the structure of 4E-BP in solution.
- Structural analysis was performed on both free and eIF4E-bound states of 4E-BP.
Main Results:
- While intrinsically disordered in its free state, 4E-BP exhibits significant compaction when bound to eIF4E.
- The SAXS data reveals a dynamic and less ordered interaction, termed a 'fuzzy complex'.
Conclusions:
- The study challenges the prevailing view of the eIF4E/4E-BP complex regulation.
- 4E-BP undergoes a conformational change upon binding, forming a 'fuzzy complex' with eIF4E.
- This finding provides new insights into the mechanism of translation regulation.
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