tRNA-tRNA interactions within cellular ribosomes.
نویسندگان
چکیده
منابع مشابه
Release of (oligo) peptidyl-tRNA from ribosomes by erythromycin A.
Erythromycin A released peptidyl-tRNA in the in vitro polypeptide synthesis system with bacterial components programmed by synthetic polynucleotide. This is consistent with our hypothesis that erythromycin A inhibits translocation by preventing proper situation of oligopeptidyl-tRNA in the donor (D) site on ribosomes.
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Programmed 30 S subunits expose only one binding site, to which the different classes of tRNA (deacylated tRNAPhe, Phe-tRNAPhe, and N-acetylphenylalanyl (AcPhe)-tRNAPhe) bind with about the same affinity. Elongation factor Tu within the ternary complex does not contribute to the binding of Phe-tRNA. Binding of acylated or deacylated tRNA to 30 S depends on the cognate codon; nonprogrammed 30 S ...
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We suggest that the interaction between a codon and its cognate tRNA induces conformational changes in the tRNA. We further suggest that sites on the ribosome preferentially bind tRNA in those conformations which require proper matching of codon and anticodon. According to this model, the codon functions as an allosteric effector which influences the conformation at various sites in the tRNA. T...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1989
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.86.12.4397