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. 1992 Feb 11;20(3):475–478. doi: 10.1093/nar/20.3.475

Recognition nucleotides for human phenylalanyl-tRNA synthetase.

I A Nazarenko 1, E T Peterson 1, O D Zakharova 1, O I Lavrik 1, O C Uhlenbeck 1
PMCID: PMC310410  PMID: 1741281

Abstract

The specificity of the interaction between tRNAPhe and phenylalanyl-tRNA synthetase isolated from human placenta was investigated. Using yeast tRNAPhe transcripts with different point mutations it was shown that all the five recognition points for the yeast phenylalanyl-tRNA synthetase (G20, G34, A35, A36 and A73) are also important for the reaction catalyzed by the human enzyme. A set of mutations in nucleotides involved in tertiary interactions of tRNAPhe revealed that mutations which maintained the proper folding of the molecule had almost no influence on the efficiency of aminoacylation. The most striking difference between the yeast and human phenylalanyl-tRNA synthetases involved a mutation in the lower two base pairs of the anticodon stem. This mutation did not affect aminoacylation with the yeast enzyme, but greatly reduced activity with human phenylalanyl-tRNA synthetase.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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