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Related Experiment Videos

Codon pair utilization biases influence translational elongation step times

B Irwin1, J D Heck, G W Hatfield

  • 1Department of Microbiology and Molecular Genetics, College of Medicine, University of California, Irvine 92717, USA.

The Journal of Biological Chemistry
|September 29, 1995
PubMed
Summary

Over-represented codon pairs in Escherichia coli are translated slower than under-represented pairs. This suggests codon usage co-evolved with transfer RNA (tRNA) abundance to regulate protein translation speed.

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Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Codon usage bias influences protein synthesis efficiency.
  • Transfer RNA (tRNA) availability and compatibility impact translation speed.
  • Ribosome dynamics are sensitive to the sequence context of codons.

Purpose of the Study:

  • To investigate the relationship between codon pair frequency and in vivo translational step times in Escherichia coli.
  • To determine if codon context affects the speed of polypeptide elongation.
  • To explore the co-evolution of codon usage and tRNA availability.

Main Methods:

  • Development and application of two independent assays to measure in vivo translational step times.
  • Analysis of codon pair frequencies in protein coding sequences of Escherichia coli.

Related Experiment Videos

  • Correlation of translational step times with codon pair over- or under-representation.
  • Main Results:

    • Over-represented codon pairs are translated significantly slower than under-represented pairs.
    • Translational step times are influenced by the compatibility of adjacent tRNA isoacceptors on the ribosome.
    • Codon pair frequency correlates with tRNA structure and abundance.

    Conclusions:

    • Codon usage frequency is a key determinant of translation speed.
    • The observed codon usage patterns are shaped by co-evolution with tRNA molecules to optimize translation.
    • This regulatory mechanism controls translation rates without altering amino acid sequences or protein structures.