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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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Translation is the process of synthesizing proteins from the genetic information carried by messenger RNA (mRNA). Following transcription, it constitutes the final step in the expression of genes. This process is carried out by ribosomes, complexes of protein and specialized RNA molecules. Ribosomes, transfer RNA (tRNA), and other proteins produce a chain of amino acids—the polypeptide—as the end product of translation.
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De novo Identification of Actively Translated Open Reading Frames with Ribosome Profiling Data
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Translational read-through promotes aggregation and shapes stop codon identity.

Lior Kramarski1, Eyal Arbely1,2

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C-terminally extended proteins, resulting from stop codon read-through, are targeted for degradation. Downstream 3'-untranslated region (UTR) sequences promote their aggregation and lysosomal targeting, revealing a novel protein quality control pathway.

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Area of Science:

  • Molecular Biology
  • Genetics
  • Cell Biology

Background:

  • Accurate translation termination is crucial for protein synthesis fidelity.
  • Errors in stop codon decoding can produce C-terminally extended proteins.
  • The cellular mechanisms for clearing these aberrant proteins remain largely unknown.

Purpose of the Study:

  • To elucidate the mechanism responsible for the sequestration and elimination of C-terminally extended proteins in eukaryotes.
  • To investigate the role of 3 on-translated region (UTR) encoded polypeptides in this process.

Main Methods:

  • Investigating the aggregation and lysosomal targeting of C-terminally extended proteins.
  • Utilizing aminoglycoside antibiotics, suppressor tRNAs, and gene knockdown to induce stop codon read-through.
  • Analyzing the correlation between termination fidelity and the predicted properties of 3 -UTR encoded polypeptides.

Main Results:

  • 3 -UTR encoded polypeptides were found to induce aggregation and lysosomal targeting of C-terminally extended proteins.
  • Protein aggregation levels varied, similar to random sequences, and could be induced by agents promoting stop codon read-through.
  • A correlation was observed between termination signal fidelity and the propensity of downstream 3 -UTR sequences to form intrinsically disordered regions.

Conclusions:

  • 3 -UTR encoded polypeptides represent a novel mechanism for promoting the aggregation and degradation of C-terminally extended proteins.
  • This pathway acts as a quality control system to prevent the accumulation of aberrant proteins.
  • The propensity for intrinsically disordered regions in 3 -UTR polypeptides may influence termination fidelity and protein quality control.