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PMID: 7015339 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 78 ·No. 3 ·1981-03-00 ·Pages 1606-8

Renaud M, Bacha H, Remy P, Ebel JP

Abstract

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 with tRNA, a structural alteration of the enzyme's active site is achieved. This process may be a determining step in the specificity of the aminoacylation reaction.

MeSH Terms
Adenosine Amino Acyl-tRNA Synthetases/metabolism Binding Sites Oligonucleotides Phenylalanine-tRNA Ligase/metabolism Protein Binding RNA, Transfer/metabolism Saccharomyces cerevisiae/enzymology Substrate Specificity
Chemicals
Oligonucleotides cytidylyl-cytidylyl-adenosine RNA, Transfer Amino Acyl-tRNA Synthetases Phenylalanine-tRNA Ligase Adenosine
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Renaud M
Bacha H
Remy P
Ebel J P
References (26)
26 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.78.3.1606
Published
1981-03-00
Pages
1606-8
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC319180
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.78.3.1606 PMC Full Text View journal details
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