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

AUTOR(ES)

Dudock, B.

RESUMO

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).

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