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Aminoacyl RNA domain of turnip yellow mosaic virus Val-RNA interacting with elongation factor Tu
Author(s) -
Rajiv L. Joshi,
Heinz G. Faulhammer,
F. Chapeville,
Mathias Sprinzl,
AnneLise Haenni
Publication year - 1984
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/12.19.7467
Subject(s) - turnip yellow mosaic virus , rna , adenylylation , ef tu , gtp' , transfer rna , biology , biochemistry , enzyme , gene , biosynthesis
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.

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