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Stoichiometry of the EF‐Tu · GTP complex with aminoacyl‐tRNA: ternary of quinternary?
Author(s) -
Leberman Reuben
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01398-k
Subject(s) - ternary complex , ef tu , gtp' , aminoacyl trna , titration , transfer rna , stoichiometry , ternary operation , elongation factor , chemistry , elongation , biochemistry , complex formation , stereochemistry , rna , enzyme , organic chemistry , inorganic chemistry , ribosome , materials science , ultimate tensile strength , computer science , programming language , metallurgy , gene
The stoichiometry of the complex formed between the Escherichia coli polypeptide elongation factor EF‐Tu, GTP and valyl‐tRNA val has been determined by non‐enzymatic deacylation studies on mixtures of the components at well‐defined concentrations. A titration end‐point was found corresponding to a 1:1 complex of EF‐Tu · GTP with the aminoacylated‐tRNA i.e. formation of a ternary complex. The result conforms to the classical model of the elongation step and not to the revolutionary proposition of the formation of a 2:2:1 complex; quinternary complex (EF‐Tu · GTP) 2 · as‐RNA.