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Selenocysteine codons decrease polysome association on endogenous selenoprotein mRNAs.

G W Martin1, M J Berry

  • 1Thyroid Division, Department of Medicine, Brigham and Women's Hospital and Harvard Medical School, Boston, MA 02115, USA.

Genes to Cells : Devoted to Molecular & Cellular Mechanisms
|March 22, 2001
PubMed
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Selenocysteine incorporation is inefficient due to a translational penalty from UGA codons in selenoprotein mRNAs. Increased release factors may improve this process for selenoprotein synthesis.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Selenocysteine incorporation into proteins is generally inefficient across various biological systems.
  • Despite observed inefficiencies, animals produce full-length selenoproteins, suggesting natural processes differ from experimental findings.

Purpose of the Study:

  • Investigate the discrepancy between observed and natural selenocysteine incorporation efficiency.
  • Analyze ribosomal loading on selenoprotein mRNAs in mammalian cells.

Main Methods:

  • Examined polysome profiles of endogenous selenoprotein mRNAs (type 1 deiodinase, glutathione peroxidase, selenoprotein P) in a mammalian cell line.
  • Compared ribosomal loading with nonselenoprotein mRNAs.
  • Substituted cysteine for selenocysteine codon in type 1 deiodinase mRNA.

Related Experiment Videos

  • Assessed the impact of eukaryotic release factors eRF1 and eRF3 expression.

    • Main Results:

    • Selenoprotein mRNAs (type 1 deiodinase, glutathione peroxidase, selenoprotein P) showed reduced ribosome loading compared to their predicted sizes.
    • Ribosome numbers correlated with UGA selenocysteine codon termination.
    • Replacing the selenocysteine codon with a cysteine codon normalized ribosomal loading.
    • Increased expression of eukaryotic release factors eRF1 and eRF3 enhanced ribosomal loading.

    Conclusions:

    • The UGA selenocysteine codon imposes a translational penalty on selenoprotein mRNAs.
    • Elevated levels of eukaryotic release factors may influence termination kinetics during selenoprotein synthesis.