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  • Title: Two GTPs are consumed on EF-Tu per peptide bond in poly(Phe) synthesis, in spite of switching stoichiometry of the EF-Tu.aminoacyl-tRNA complex with temperature.
    Author: Dinçbaş V, Bilgin N, Scoble J, Ehrenberg M.
    Journal: FEBS Lett; 1995 Jan 02; 357(1):19-22. PubMed ID: 8001671.
    Abstract:
    Recent observations indicate that the stoichiometry for the complex between EF-Tu.GTP and aminoacyl-tRNA (aa-tRNA) changes with temperature. At 37 degrees C two EF-Tu.GTPs bind one aa-tRNA in an extended ternary complex, but at 0 degrees C the complex has 1:1 stoichiometry. However, the present experiments show that there are two GTPs hydrolyzed on EF-Tu per peptide bond in poly(Phe) synthesis at 37 degrees C as well as at 0 degrees C. This indicates two different pathways for the enzymatic binding of aa-tRNA to the A-site on the ribosome.
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