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

• Published in: FEBS letters Vol. 196; no. 1; pp. 103 - 107
• Main Authors: Kakhniashvili, D.G., Smailov, S.K., Gavrilova, L.P.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 03-02-1986; Elsevier
• Subjects: Applied sciences; Biological and medical sciences; Elongation factor Tu function; Escherichia coli - metabolism; Exact sciences and technology; Fundamental and applied biological sciences. Psychology; Guanosine Triphosphate - metabolism; Hydrolysis; Misreading; Molecular and cellular biology; Molecular genetics; Other techniques and industries; Peptide Biosynthesis; Peptide Chain Elongation, Translational; Peptide Elongation Factor Tu - metabolism; Peptides; Poly (U)-Sepharose translation system; Poly U - genetics; Proof-reading; Ribosomes - metabolism; RNA, Transfer, Amino Acyl - metabolism; Substrate Specificity; Translation. Translation factors. Protein processing; Misreading; Poly (U)-Sepharose translation system; Proof-reading; Elongation factor Tu function; Hydrolysis; GTP; Ribosome; In vitro translation; T RNA; Elongation factor EFTu
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(86)80222-8

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.