Binding of yeast tRNAphe anticodon arm to Escherichia coli 30 S ribosomes

Samuel J. Rose*, Peggy T. Lowary, Olke C. Uhlenbeck

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

49 Scopus citations

Abstract

A 15-nucleotide fragment of RNA having the sequence of the anticodon arm of yeast tRNAPhe was constructed using T4 RNA ligase. The stoichiometry and binding constant of this oligomer to poly(U)-programmed 30 S ribosomes was found to be identical to that of deacylated tRNAPhe. The anticodon arm and tRNAPhe also compete for the same binding site on the ribosome. These data indicate that the interaction of tRNAPhe with poly(U)-programmed 30 S ribosomes is primarily a result of contacts in the anticodon arm region and not with other parts of the transfer RNA. Since similar oligomers which cannot form a stable helical stem do not bind ribosomes, a clear requirement for the entire anticodon arm structure is demonstrated.

Original languageEnglish (US)
Pages (from-to)103-117
Number of pages15
JournalJournal of Molecular Biology
Volume167
Issue number1
DOIs
StatePublished - Jun 15 1983

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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