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Related Experiment Videos

Selenocysteine insertion or termination: factors affecting UGA codon fate and complementary anticodon:codon mutations

M J Berry1, J W Harney, T Ohama

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

Nucleic Acids Research
|September 11, 1994
PubMed
Summary

Selenocysteine incorporation, where UGA signals selenocysteine instead of termination, is influenced by both selenoprotein DNA and tRNA levels. Maintaining codon:anticodon complementarity is key for this process in mammalian cells.

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Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • The translation of the UGA codon as selenocysteine, rather than termination, is crucial for numerous proteins.
  • Eukaryotic mRNAs utilize 3' untranslated region stem-loops for this specific UGA decoding.
  • Selenocysteine incorporation efficiency is often suboptimal despite the presence of these signals.

Purpose of the Study:

  • To investigate factors limiting selenocysteine incorporation efficiency.
  • To determine the impact of deiodinase cDNA and selenocysteine tRNA concentrations on UGA readthrough.
  • To elucidate the role of codon:anticodon complementarity in selenocysteine incorporation.

Main Methods:

  • Transfection of cells with deiodinase cDNA and selenocysteine-specific tRNA genes.

Related Experiment Videos

  • Quantification of full-length and UGA-terminated protein products via Western blotting.
  • Analysis of selenocysteine incorporation efficiency under varying selenium concentrations and codon mutations.

    • Main Results:

    • Both selenoprotein DNA and tRNA concentrations significantly affect the ratio of selenocysteine incorporation to termination.
    • Selenium depletion reduces UGA readthrough, indicating its importance in the process.
    • UGA is not essential for selenocysteine incorporation if codon:anticodon complementarity is maintained, as shown by mutation studies.

    Conclusions:

    • Selenocysteine incorporation efficiency is modulated by the availability of both the selenoprotein mRNA template and the cognate tRNA.
    • The UGA codon can function as both a stop and a selenocysteine codon within the same mRNA.
    • Maintaining precise codon:anticodon pairing is critical for accurate selenocysteine insertion in mammalian systems.