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Related Concept Videos

Protein Modifications in the RER01:26

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Base complementarity between the three base pairs of mRNA codon and the tRNA anticodon is not a failsafe mechanism. Inaccuracies can range from a single mismatch to no correct base pairing at all. The free energy difference between the correct and nearly correct base pairs can be as small as 3 kcal/ mol. With complementarity being the only proofreading step, the estimated error frequency would be one wrong amino acid in every 100 amino acids incorporated. However, error frequencies observed in...
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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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eIF3 Interacts with Selenoprotein mRNAs.

Hassan Hayek1,2, Gilbert Eriani1, Christine Allmang1

  • 1Architecture et Réactivité de l'ARN, Université de Strasbourg, Centre National de la Recherche Scientifique, Institut de Biologie Moléculaire et Cellulaire, 67084 Strasbourg, France.

Biomolecules
|September 23, 2022
PubMed
Summary

Eukaryotic translation initiation factor 3 (eIF3) interacts with specific selenoprotein mRNAs, particularly those with unusual cap hypermethylation. This suggests eIF3 may regulate selenoprotein expression independently of the typical translation initiation factor 4E (eIF4E).

Keywords:
GPx1RNA-protein interactioneukaryotic initiation factorselenoprotein mRNAtranslation regulation

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Area of Science:

  • Molecular Biology
  • Gene Expression Regulation
  • Protein Synthesis

Background:

  • Selenoprotein synthesis relies on co-translational recoding of UGA codons.
  • Selenocysteine insertion involves SECIS element and SBP2 protein interactions.
  • Some selenoprotein mRNAs are translated despite lacking eIF4E recognition due to cap hypermethylation.

Purpose of the Study:

  • To investigate the interaction between human eukaryotic translation initiation factor 3 (eIF3) and selenoprotein mRNAs.
  • To determine if eIF3 plays a role in the specialized translation of selenoprotein mRNAs.
  • To elucidate the mechanisms of selenoprotein translation regulation.

Main Methods:

  • Ribonucleoprotein immunoprecipitation (RNP IP) in vivo and in vitro.
  • Cross-linking experiments to identify direct interactions.
  • Analysis of interactions between eIF3 subunits and specific selenoprotein mRNAs (e.g., GPx1 mRNA).

Main Results:

  • eIF3 interacts with a subset of selenoprotein mRNAs.
  • eIF3 preferentially binds to hypermethylated capped selenoprotein mRNAs over m7G-capped mRNAs.
  • Direct contacts were identified between GPx1 mRNA and eIF3 subunits c, d, and e.
  • Common interaction patterns were observed for hypermethylated capped selenoprotein mRNAs.

Conclusions:

  • Differential interactions of eIF3 with selenoprotein mRNAs suggest novel translation pathways.
  • eIF3 may regulate selenoprotein expression independently of eIF4E.
  • eIF3 emerges as a potential key regulator in the hierarchy of selenoprotein expression.