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Related Experiment Videos

Cytoplasmic complex of p53 and eEF2.

Xia Yin1, Beatriz M A Fontoura, Takashi Morimoto

  • 1Department of Pathology, New York University School of Medicine, New York, New York, USA.

Journal of Cellular Physiology
|August 2, 2003
PubMed
Summary
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The tumor suppressor p53 protein binds to elongation factor eEF2 and 5.8S rRNA, suggesting p53 regulates protein translation elongation. This interaction changes when p53 moves to the nucleus.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Cytoplasmic p53 has been previously linked to 5.8S rRNA and polyribosomes translating p53 mRNA.
  • 5.8S rRNA's location suggests a role for p53 in translational regulation.

Purpose of the Study:

  • To investigate the interaction between p53 and eukaryotic elongation factor 2 (eEF2).
  • To elucidate the role of p53 in protein translation elongation.

Main Methods:

  • Co-immunoprecipitation assays to detect p53-eEF2 complex formation.
  • Sucrose gradient sedimentation to analyze the localization of p53 and eEF2.
  • Diphtheria toxin (DT) and gamma-32P-azido-GTP assays to identify and characterize eEF2.
  • Cycloheximide (Cx) sensitivity assays to assess translational effects.

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Main Results:

  • p53 forms a salt-stable complex with eEF2, identified as a 97 kDa protein.
  • p53 and eEF2 are found in both polyribosomal and subribosomal fractions.
  • Subribosomal p53 can bind eEF2 independently of ribosomes.
  • eEF2 binding to p53 decreases as p53 translocates to the nucleus.
  • p53 influences the sensitivity of p53 mRNA translation to the elongation inhibitor cycloheximide.

Conclusions:

  • p53 associates with key translational machinery components, including eEF2 and 5.8S rRNA.
  • These interactions suggest a novel role for p53 in regulating translational elongation.
  • The dynamic binding of eEF2 to p53, dependent on p53's cellular localization, highlights a regulatory mechanism.