Abstract

Efficient aminoacylation of an RNA minihelix (a proposed precursor of tRNA) was achieved without any ribozymes or protein enzymes. The reaction was promoted with a template-like bridging Oligonucleotide and a 5'-aminoacyl-phosphate-oligonucleotide. Aminoacylation was template-dependent and showed high preference for a particular ribose hydroxyl. The 5'-aminoacyl-phosphate-oligonucleotides have the same adenylate linkage as in aminoacyl-AMP--the universal intermediate used in modern aminoacylation systems with aminoacyl-tRNA synthetases. Thus, the results raise the possibility that this kind of system could have played a role in the transition from the RNA world to the theatre of proteins.

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