Abstract
THE optimum efficiency of protein biosynthesis depends on the availability of aminoacyl-transfer RNAs (tRNAs) in the neighbourhood of active polysomes, among other factors. The intracellular tRNA level is directly proportional to the composition of the amino acids incorporated into proteins being synthesised1. This continuous and selective adjustment takes place in prokaryotes and eukaryotes and in non-differentiated as well as in highly specialised cell systems2. We report here that such a proportionality takes place at the molecular level between the frequency of synoinomous codons in messenger RNAs (mRNAs) and the distribution of the corresponding isoacceptor tRNAs. A correlation was found for the alanine, glycine and serine codons from viral nucleic acids and eukaroytic iso-tRNA sets fractionated on reversed-phase chromatography as well as for the preponderant tRNAs involved in the translation of fibroin mRNA in the posterior silk gland of the silkworm Bombyx mori L.
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GAREL, JP. Quantitative adaptation of isoacceptor tRNAs to mRNA codons of alanine, glycine and serine. Nature 260, 805–806 (1976). https://doi.org/10.1038/260805a0
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DOI: https://doi.org/10.1038/260805a0
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