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2) How does such a model permit codon assignments to be altered? And, (3) can a codon catalog be evolved by such a route in a finite amount of time? [WOESE, 1967 (1)]. , each (right) step in the process conferring upon the cell a very slight selective advantage. Thus we can argue in keeping with the first objection that since the selective advantage gained at each step is so slight, this evolution of the code can in no way preclude the evolution in cells of other, unrelated structures and functions.
In principle such an evolution seems straightforward, in that it is a simple extrapolation from the basic interaction - just as is the case for nucleic acid replication and base pairing. As we have seen above, there exists no evidence for a strong "codon-amino acid pairing" interaction, so that one has to view evolution as starting with a weak interaction of this sort and then amplifying it, bringing it out, into an all-or-none process. Provided these weak interactions did exist the major question is then how on such a model one gets from a more-or-Iess direct templating mechanism to the present mechanism, in which the amino acid associates with the codon only through the allimportant intermediary, the tRNA "adaptor" system.
BERG, and M. DIECKMANN: The enzymic synthesis of amino acyl derivatives of ribonucleic acid. J. bioI. Chem. 236, 1735-1740 (1961). , and M. W. NIRENBERG: Science 147, 479 (1965). , J. LEAHY, and R. SCHWEET: Formation of the peptide chain of hemoglobin. Proc. nat. Acad Sci. ) 46, 1030-1038 (1960). BRAMMER, W. , H. BERGER, and C. YANOFSKY: Altered amino acid sequences produced by reversion of frameshift mutants of tryptophan synthetase A gene of E. coli. Proc. nat. Acad. Sci. ) 58, 1499-1506 (1967).