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Mutations in 16S rRNA that affect UGA (stop codon)-directed translation termination.

H U Göringer1, K A Hijazi, E J Murgola

  • 1Max-Planck-Institut für Molekulare Genetik, Abteilung Wittmann, Berlin, Federal Republic of Germany.

Proceedings of the National Academy of Sciences of the United States of America
|August 1, 1991
PubMed
Summary

Mutagenesis of Escherichia coli 16S rRNA

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Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Peptide chain termination is a critical process in protein synthesis.
  • The 3' major domain of Escherichia coli 16S rRNA is implicated in termination.
  • Previous studies suggested a role for rRNA in termination signals.

Purpose of the Study:

  • To investigate the role of a specific sequence motif in Escherichia coli 16S rRNA in peptide chain termination.
  • To elucidate the mechanism of UGA stop codon recognition during termination.

Main Methods:

  • Site-directed mutagenesis was used to alter the 16S rRNA sequence motif.
  • Analysis of stop codon suppression in mutant ribosomes was performed.
  • Ribosome function, including initiation and elongation, was assessed.

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Main Results:

  • Mutations exclusively affected UGA stop signal recognition.
  • The UGA response correlated with the integrity of tandem UCA sequences (bases 1199-1204).
  • Ribosome initiation and elongation remained functional in mutants.

Conclusions:

  • A direct interaction between the UGA stop codon and the 16S rRNA UCA motif is proposed for UGA-dependent termination.
  • Base pairing between rRNA and mRNA plays a direct role in peptide chain termination.
  • This interaction is a key event in initiating UGA-dependent peptide chain termination.