Idiosyncratic tuning of tRNAs to achieve uniform ribosome binding

Mikołaj Olejniczak, Taraka Dale, Richard P. Fahlman, Olke C. Uhlenbeck*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

72 Scopus citations

Abstract

The binding of seven tRNA anticodons to their complementary codons on Escherichia coli ribosomes was substantially impaired, as compared with the binding of their natural tRNAs, when they were transplanted into tRNA 2Ala. An analysis of chimeras composed of tRNA 2Ala and various amounts of either tRNA3 Gly or tRNA2Arg indicates that the presence of the parental 32-38 nucleotide pair is sufficient to restore ribosome binding of the transplanted anticodons. Furthermore, mutagenesis of tRNA2 Ala showed that its highly conserved A32-U38 pair serves to weaken ribosome affinity. We propose that this negative binding determinant is used to offset the very tight codon-anticodon interaction of tRNA2 Ala. This suggests that each tRNA sequence has coevolved with its anticodon to tune ribosome affinity to a value that is the same for all tRNAs.

Original languageEnglish (US)
Pages (from-to)788-793
Number of pages6
JournalNature Structural and Molecular Biology
Volume12
Issue number9
DOIs
StatePublished - Sep 1 2005

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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