Utilization of isomeric aminoacyl transfer ribonucleic acids in peptide bond formation

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

To the extent that the results obtained for the modified tRNAs are applicable to the corresponding unmodified species, several conclusions may be drawn. For example, while the initial position of tRNA aminoacylation shows considerable diversity from one isoacceptor to another, the aminoacylation of any single tRNA is probably specific for a single hydroxyl group at the 3′ terminus of tRNA. Moreover, that specificity has generally been conserved through the evolution from prokaryotic to mammalian species. Both positional isomers of tRNA can bind to EF-Tu-GTP, although it is possible that one isomer may normally be bound preferentially. Similarly, both of the modified 2′- and 3′-aminoacyl-tRNA analogues were bound equally to both the A and the P sites, although neither analogue was bound as well to the P site as the corresponding unmodified tRNA. While the acceptor species in the peptidyltransferase reaction is almost certainly the 3′-O-aminoacyl derivative, it has not been possible to determine which positional isomer acts as the donor. It seems reasonable to conclude that there is positional specificity in those partial reactions of protein biosynthesis which involve formation or breaking of the O-acyl bond, but much less specificity when only the binding of aminoacyl(peptidyl)-tRNA is involved.

Original languageEnglish (US)
Pages (from-to)239-245
Number of pages7
JournalAccounts of Chemical Research
Volume10
Issue number7
StatePublished - 1977
Externally publishedYes

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Transfer RNA
Peptides
Isomers
Peptide Elongation Factor Tu
Peptidyl Transferases
Biosynthesis
Guanosine Triphosphate
Hydroxyl Radical
Derivatives
Proteins

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Utilization of isomeric aminoacyl transfer ribonucleic acids in peptide bond formation. / Hecht, Sidney.

In: Accounts of Chemical Research, Vol. 10, No. 7, 1977, p. 239-245.

Research output: Contribution to journalArticle

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