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Conformational Ensembles of the Disordered 4E-BP2:eIF4E Complex Restrained by smFRET Experiments.

Spencer Smyth1,2, Zi Hao Liu3,4, Thomas E Tsangaris1,2

  • 1Department of Physics, University of Toronto, Toronto, Ontario, M5S 1A7, Canada.

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Eukaryotic translation initiation involves eukaryotic initiation factor 4E (eIF4E) binding to 4E proteins. This study reveals new contact regions in the dynamic 4E-BP2:eIF4E complex, impacting translation regulation.

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clustering analysiscontact mapsintegrative modellingintrinsically disordered proteinssingle-molecule fluorescence

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biophysics

Background:

  • Eukaryotic translation initiation is a key regulatory point in gene expression.
  • Eukaryotic initiation factor 4E (eIF4E) binding to 4E-binding proteins (4E-BPs) regulates this process.
  • 4E-BPs are intrinsically disordered proteins, posing challenges for structural determination.

Purpose of the Study:

  • To generate and analyze atomistic conformational ensembles of 4E-BP2 and its complex with eIF4E.
  • To compare the structural dynamics of free 4E-BP2 and its bound state.
  • To elucidate the structural basis of translation regulation by the 4E-BP2:eIF4E complex.

Main Methods:

  • IDPConformerGenerator and X-EISDv2 workflow for generating conformational ensembles.
  • Integration of single-molecule fluorescence and NMR data.
  • Validation using solution spectroscopy and comparison with crystal structure data.

Main Results:

  • Generated full-length atomistic conformational ensembles for apo 4E-BP2 and the 4E-BP2:eIF4E complex.
  • Observed delocalization of contacts and identified two new contact regions between disordered termini.
  • Validated ensemble models with experimental data, supporting a dynamic binding interface.

Conclusions:

  • The dynamic nature of the 4E-BP2:eIF4E complex is crucial for translation regulation.
  • Newly identified contact regions suggest allosteric roles in modulating binding affinity.
  • The findings support a model where the complex's dynamics facilitate regulatory site accessibility.