Stoichiometry of the EF-Tu.GTP complex with aminoacyl-tRNA: ternary of quinternary?
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.
Leberman
R
R
European Molecular Biology Laboratory, Grenoble Outstation, France.
D004926:Escherichia coli / Q000737:chemistry; D006160:Guanosine Triphosphate / Q000737:chemistry / Q000378:metabolism*; D007700:Kinetics; D008956:Models, Chemical; D010441:Peptide Chain Elongation, Translational; D010444:Peptide Elongation Factor Tu / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation; D012346:RNA, Transfer, Amino Acyl / Q000737:chemistry / Q000378:metabolism*; D017186:Titrimetry
D012346:RNA, Transfer, Amino Acyl; D006160:Guanosine Triphosphate; D010444:Peptide Elongation Factor Tu