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Related Experiment Video

Updated: Jul 11, 2026

Identification of Protein Interacting Partners Using Tandem Affinity Purification
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Crystal structure of eIF2B and insights into eIF2-eIF2B interactions.

Kazuhiro Kashiwagi1, Takuhiro Ito1, Shigeyuki Yokoyama2

  • 1Division of Structural and Synthetic Biology, RIKEN Center for Life Science Technologies, Tsurumi-ku, Yokohama, Japan.

The FEBS Journal
|September 15, 2016
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Summary

Eukaryotic translation initiation factor 2B (eIF2B) regulates protein synthesis. Stress-induced eIF2α phosphorylation inhibits eIF2B

Keywords:
X-ray crystallographyeIF2Beukaryotic translation initiation factorguanine nucleotide exchange factortranslational control

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Eukaryotic translation initiation factor 2B (eIF2B) is a guanine nucleotide exchange factor (GEF) essential for protein synthesis.
  • eIF2B regulates the activity of eIF2, a heterotrimeric G protein involved in delivering initiator tRNA to the ribosome.
  • Stress-induced phosphorylation of eIF2α inhibits eIF2B GEF activity, leading to global translation repression.

Purpose of the Study:

  • To elucidate the structural mechanism of eIF2B's GEF activity inhibition.
  • To determine the three-dimensional structure of the eIF2B complex.
  • To understand how eIF2α phosphorylation affects eIF2B structure and function.

Main Methods:

  • Crystal structure determination of Schizosaccharomyces pombe eIF2B.
  • Structure-based in vitro analyses.
  • Biochemical assays to assess GEF activity.

Main Results:

  • The crystal structure of eIF2B reveals its heterodecameric architecture.
  • Structural insights into the mechanism of GEF activity inhibition by phosphorylated eIF2α.
  • Demonstration of how phosphorylation impacts eIF2B's interaction with eIF2.

Conclusions:

  • The study provides a structural basis for understanding translation regulation by eIF2B.
  • Elucidates the mechanism by which stress signaling inhibits protein synthesis.
  • Offers potential targets for therapeutic interventions related to translation control.