Idiosyncratic tuning of tRNAs to achieve uniform ribosome binding

Mikołaj Olejniczak; Taraka Dale; Richard P. Fahlman; Olke C. Uhlenbeck

doi:10.1038/nsmb978

Idiosyncratic tuning of tRNAs to achieve uniform ribosome binding

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

^*Corresponding author for this work

Molecular Biosciences

Research output: Contribution to journal › Article › peer-review

84 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 ₂^Ala. An analysis of chimeras composed of tRNA ₂^Ala and various amounts of either tRNA₃ ^Gly or tRNA₂^Arg 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 language	English (US)
Pages (from-to)	788-793
Number of pages	6
Journal	Nature Structural and Molecular Biology
Volume	12
Issue number	9
DOIs	https://doi.org/10.1038/nsmb978
State	Published - Sep 2005

Funding

This work was supported by US National Institutes of Health Grant GM 37552 to O.C.U. We would also like to thank M. Saks for critically reading the manuscript.

ASJC Scopus subject areas

Molecular Biology
Structural Biology

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10.1038/nsmb978

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title = "Idiosyncratic tuning of tRNAs to achieve uniform ribosome binding",

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.",

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AU - Olejniczak, Mikołaj

AU - Dale, Taraka

AU - Fahlman, Richard P.

AU - Uhlenbeck, Olke C.

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AB - 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.

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Idiosyncratic tuning of tRNAs to achieve uniform ribosome binding

Abstract

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