The excess GTP hydrolyzed during mistranslation is expended at the stage of EF-Tu-promoted binding of non-cognate aminoacyl-tRNA.
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 codon-specific elongation (polyphenylalanine synthesis) and misreading (polyleucine synthesis). 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.
D004926:Escherichia coli / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000378:metabolism*; D006868:Hydrolysis; D010452:Peptide Biosynthesis; D010441:Peptide Chain Elongation, Translational; D010444:Peptide Elongation Factor Tu / Q000378:metabolism*; D010455:Peptides; D011072:Poly U / Q000235:genetics; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism; D013379:Substrate Specificity
D010455:Peptides; D012346:RNA, Transfer, Amino Acyl; C027819:polyleucine; D011072:Poly U; C012001:polyphenylalanine; D006160:Guanosine Triphosphate; D010444:Peptide Elongation Factor Tu