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Yeast As a Chassis for Developing Functional Assays to Study Human P53
14:57

Yeast As a Chassis for Developing Functional Assays to Study Human P53

Published on: August 4, 2019

p53 directs conformational change and translation initiation blockade of human fibroblast growth factor 2 mRNA

B Galy1, L Créancier, L Prado-Lourenço

  • 1Institut National de la Santé et de la Recherche Médicale U397, Endocrinologie et Communication Cellulaire, Institut Fédératif de Recherche Louis Bugnard, C.H.U. Rangueil, 31403 Toulouse Cedex 04, France.

Oncogene
|August 11, 2001
PubMed

Insights

Tumor suppressor p53 inhibits fibroblast growth factor 2 (FGF-2) mRNA translation by blocking ribosome formation. This repression involves p53-induced RNA structural changes in the FGF-2 mRNA leader sequence.

Area of Science:

  • Molecular Biology
  • RNA Biology
  • Cancer Research

Background:

  • Tumor suppressor p53 is known to inhibit fibroblast growth factor 2 (FGF-2) expression post-transcriptionally.
  • The precise mechanism underlying this p53-mediated post-transcriptional regulation of FGF-2 remains to be fully elucidated.

Purpose of the Study:

  • To investigate the molecular mechanism by which p53 represses FGF-2 mRNA translation.
  • To identify the specific RNA elements and p53 activities involved in this translational blockade.

Main Methods:

  • Deletion mutagenesis of the FGF-2 mRNA leader sequence.
  • In vitro translation assays using rabbit reticulocyte lysate.
  • Sucrose gradient centrifugation to analyze ribosome formation.
  • RNA accessibility assays using complementary oligonucleotide probes.

Main Results:

  • At least four cis-acting RNA elements within the FGF-2 mRNA leader are required for p53-mediated inhibition.
  • Wild-type p53, but not a specific mutant (Ala143), repressed FGF-2 mRNA translation in a dose-dependent manner.
  • p53 blocks translation initiation by preventing 80S ribosome complex formation.
  • p53 binding induced conformational changes in the FGF-2 mRNA leader, correlating with translational repression, independent of direct RNA binding affinity.

Conclusions:

  • p53 directly represses FGF-2 mRNA translation through a mechanism involving its nucleic acid unwinding-annealing activity.
  • p53-induced structural alterations in the FGF-2 mRNA leader likely disrupt translation initiation.
  • This study reveals a novel mechanism of translational control by p53 impacting FGF-2 expression.

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