The excess GTP hydrolyzed during mistranslation is expended at the stage of EF‐Tu‐promoted binding of non‐cognate aminoacyl‐tRNA

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Abstract
The system of translation of Sepharose-bound poly(U) in which all ribosomes are active in peptide elongation was used to determine the stoichiometry of GTP hydrolysis at the stage of EF-Tu-promoted aminoacyl-tRNA binding. The ratio of GTP hydrolyzed at this stage per peptide bond was assayed during codonspecific elongation (polyphenylalanine synthesis) and misreading (polyleucine sythesis). It was demonstrated directly that the excess GTP hydrolyzed during misreading [(1984) FEBS Letters 178, 283-287] is expended at the stage of Ef-Tu-promoted binding of non-cognate aminoacyl-tRNA.