A model for the coevolution of the genetic code and the process of protein synthesis: Review and assessment

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Abstract
The contemporary genetic code and the process of protein biosynthesis most assuredly evolved from a simpler code and process. We believe that there was obligatory coevolution of the two and that the earlier code and process must have involved a more direct linkage between the amino acids and the informational macromolecule. We propose that an early form of translating existed in which amino acids were attached directly to the ‘messenger’ RNA along the backbone as 2'OH aminoacyl esters. These esters then condensed with each other on the RNA backbone yielding a peptide covalently attached to the RNA, without the use of tRNAs and ribosomes. This presentation is concerned with experimental data which indicate that such a simple translation system is possible and must have involved the following steps: (1) formation of the aminoacyl adenylate anhydride, (2) transfer of the amino acid from the adenylate to imidazole, (3) transfer of the amino acid from imidazole to 2'OH groups along the backbone of RNAs (4) condensation of the amino acids to yield peptides. Steps (1)–(3) have been confirmed in chemical systems. Our preliminary evidence indicates step (4) is also possible. The aminoacylation of polyribonucleotides and the subsequent formation of peptides is a dynamic and experimentally accessible system for studying genetic coding specifities and our present studies are now concentrated on step (4), looking for such specifities.

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