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. 1971 Mar;68(3):681–684. doi: 10.1073/pnas.68.3.681

The Yeast Phenylalanyl-Transfer RNA Synthetase Recognition Site: The Region Adjacent to the Dihydrouridine Loop

B Dudock 1, C DiPeri 1, K Scileppi 1, R Reszelbach 1
PMCID: PMC389016  PMID: 5276781

Abstract

Purified yeast phenylalanyl-tRNA synthetase can aminoacylate (yeast) tRNAPhe, (wheat) tRNAPhe, and (Escherichia coli) tRNA1Val (1, 2). We now report that this synthetase can also aminoacylate (E. coli) tRNAPhe and (E. coli) tRNA1Ala. Highly purified (E. coli) tRNAPhe is heterologously aminoacylated to approximately 90% of the extent achieved with the homologous enzyme (crude E. coli phenylalanyl-tRNA synthetase). Pure (E. coli) tRNA1Ala (the major species) is heterologously aminoacylated to 70% of the extent achieved with the homologous synthetase (crude E. coli alanyl-tRNA synthetase).

(E. coli) tRNAPhe is the fourth purified transfer RNA of known sequence to be shown to be an acceptable substrate for purified yeast phenylalanyl-tRNA synthetase. A comparison of these sequences shows that only one region is extremely similar in all four tRNAs. This region is located adjacent to the dihydrouridine loop, and consists of the nucleotides [Formula: see text] We conclude that this is the synthetase recognition site for yeast phenylalanyl-tRNA synthetase.

This conclusion is further supported by partial fragment analysis of (E. coli) tRNA1Ala.

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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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