Conformational activation of the yeast phenylalanyl-tRNA synthetase catalytic site induced by tRNAPhe interaction: triggering of adenosine or CpCpA trinucleoside diphosphate aminoacylation upon binding of tRNAPhe lacking these residues.

Adenosine or CpCpA trinucleoside diphosphate can be aminoacylated by phenylalanyl-tRNA synthetase [L-phenylalanine:tRNAPhe ligase (AMP forming), EC 6.1.1.20] when the reaction takes place in the presence of tRNAPhe deprived of its 3' adenosine or pCpCpA terminus. This shows that, upon interacti...

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Bibliografische gegevens
Hoofdauteurs: Renaud, M, Bacha, H, Remy, P, Ebel, J P
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: 1981
Onderwerpen:
Research Article
Online toegang:https://ncbi.nlm.nih.gov/pmc/articles/PMC319180/
https://ncbi.nlm.nih.gov/pubmed/7015339
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