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 language | English (US) |
|---|---|
| Pages (from-to) | 239-245 |
| Number of pages | 7 |
| Journal | Accounts of Chemical Research |
| Volume | 10 |
| Issue number | 7 |
| State | Published - 1977 |
| Externally published | Yes |
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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 journal › Article
}
TY - JOUR
T1 - Utilization of isomeric aminoacyl transfer ribonucleic acids in peptide bond formation
AU - Hecht, Sidney
PY - 1977
Y1 - 1977
N2 - 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.
AB - 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.
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M3 - Article
AN - SCOPUS:2842594200
VL - 10
SP - 239
EP - 245
JO - Accounts of Chemical Research
JF - Accounts of Chemical Research
SN - 0001-4842
IS - 7
ER -