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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 interaction wi...

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書目詳細資料
發表在:Proc Natl Acad Sci U S A
Principais autores: Renaud, M, Bacha, H, Remy, P, Ebel, J P
格式: Artigo
語言:Inglês
出版: National Academy of Sciences 1981
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在線閱讀:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC319180/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/7015339/
https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.78.3.1606
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