Aminoacyl RNA domain of turnip yellow mosaic virus Val-RNA interacting with elongation factor Tu

Turnip yellow mosaic virus (TYMV) Val-RNA forms a complex with the peptide elongation factor Tu (EF-Tu) in the presence of GTP: the Val-RNA is protected by EF-Tu·GTP from non-enzymatic deacylation and nuclease digestion. The determination of the length of the shortest TYMV Val-RNA fragment that bind...

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Main Authors: Joshi, Rajiv L., Faulhammer, Heinz, Chapeville, François, Sprinzl, Mathias, Haenni, Anne-Lise
Formato: Artigo
Idioma:en
Publicado em: 1984
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC320175/
https://ncbi.nlm.nih.gov/pubmed/16617475
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spelling pubmed-3201752004-02-10 Aminoacyl RNA domain of turnip yellow mosaic virus Val-RNA interacting with elongation factor Tu Joshi, Rajiv L. Faulhammer, Heinz Chapeville, François Sprinzl, Mathias Haenni, Anne-Lise Nucleic Acids Res Turnip yellow mosaic virus (TYMV) Val-RNA forms a complex with the peptide elongation factor Tu (EF-Tu) in the presence of GTP: the Val-RNA is protected by EF-Tu·GTP from non-enzymatic deacylation and nuclease digestion. The determination of the length of the shortest TYMV Val-RNA fragment that binds EF-Tu·GTP leads us to conclude that the valylated aminoacyl RNA domain equivalent in tRNAs to the continuous helix formed by the acceptor stem and the T arm is sufficient for complex formation. Since the aminoacyl RNA domain is also sufficient for adenylation by the ATP(CTP):tRNA nucleotidyltransferase, an analogy can be drawn between these two tRNA-specific proteins. 1984-10-11 /pmc/articles/PMC320175/ /pubmed/16617475 Text en © IRL Press Limited, Oxford, England
institution US National Library of Medicine
collection PubMed Central
language en
format Article
description Turnip yellow mosaic virus (TYMV) Val-RNA forms a complex with the peptide elongation factor Tu (EF-Tu) in the presence of GTP: the Val-RNA is protected by EF-Tu·GTP from non-enzymatic deacylation and nuclease digestion. The determination of the length of the shortest TYMV Val-RNA fragment that binds EF-Tu·GTP leads us to conclude that the valylated aminoacyl RNA domain equivalent in tRNAs to the continuous helix formed by the acceptor stem and the T arm is sufficient for complex formation. Since the aminoacyl RNA domain is also sufficient for adenylation by the ATP(CTP):tRNA nucleotidyltransferase, an analogy can be drawn between these two tRNA-specific proteins.
author Joshi, Rajiv L.
Faulhammer, Heinz
Chapeville, François
Sprinzl, Mathias
Haenni, Anne-Lise
spellingShingle Joshi, Rajiv L.
Faulhammer, Heinz
Chapeville, François
Sprinzl, Mathias
Haenni, Anne-Lise
Aminoacyl RNA domain of turnip yellow mosaic virus Val-RNA interacting with elongation factor Tu
author_facet Joshi, Rajiv L.
Faulhammer, Heinz
Chapeville, François
Sprinzl, Mathias
Haenni, Anne-Lise
author_sort Joshi, Rajiv L.
title Aminoacyl RNA domain of turnip yellow mosaic virus Val-RNA interacting with elongation factor Tu
title_short Aminoacyl RNA domain of turnip yellow mosaic virus Val-RNA interacting with elongation factor Tu
title_full Aminoacyl RNA domain of turnip yellow mosaic virus Val-RNA interacting with elongation factor Tu
title_fullStr Aminoacyl RNA domain of turnip yellow mosaic virus Val-RNA interacting with elongation factor Tu
title_full_unstemmed Aminoacyl RNA domain of turnip yellow mosaic virus Val-RNA interacting with elongation factor Tu
title_sort aminoacyl rna domain of turnip yellow mosaic virus val-rna interacting with elongation factor tu
publishDate 1984
url https://ncbi.nlm.nih.gov/pmc/articles/PMC320175/
https://ncbi.nlm.nih.gov/pubmed/16617475
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