Stoichiometry of the EF‐Tu · GTP complex with aminoacyl‐tRNA: ternary of quinternary?
R. Leberman
Abstract
Open-access reader
R. Leberman
Abstract
Open-access reader
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.aa-RNA.
OpenAlex reports 6 citations for this work. Citation counts describe recorded attention and do not establish research quality.
A contribution statement is not available in the OpenAlex record.
Method details are not available in the OpenAlex metadata.
Findings are not separately available in the OpenAlex metadata.
Limitations are not available in the OpenAlex metadata.
Application details are not available in the OpenAlex metadata.
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.aa-RNA.
Key concepts: Ternary complex, EF-Tu, GTP', Aminoacyl-tRNA, Titration, Transfer RNA, Stoichiometry, Ternary operation