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By James Ofengand (auth.), R. Pérez-Bercoff (eds.)
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N. arassa mitochondria have ml G37 , while bean chloroplast has A37 , llke the prokaryotes. Initiator tRNA. The essential functional di~tinction between eukaryotic initiator tRNAMet and elongator tRNAMe is that one can participate in the formation of initiation complexes while the other cannot, and conversely, elongator tRNA is preferred over initiator tRNA in the formation of EFT complexes destined for binding to the ribosomal A site (2). Structurally, the main difference between initiator and elongator tRNA lies in loop IV, residues 54-60.
TRNA AND AMINOACYL SYNTHETASES 27 Met Thr. (0-70 4 kd ) , except for EC and E wh~ch appear to be made up of 2 al class subunits. ) This has raised the possibility that the a~hain is actually made up of two primordial subunits of the a2 size which have become covalently joined by gene duplication and fusion. Two lines of evidence support this concept. First, in a number of instances, very mild proteolysis cleaves al synthetases into two fragments, which in combination, sometimes retain partial enz~atic activity (2, 4).
However, the wide distribution of these complexes in many kinds of tissue makes it unlikely that this explanation will be generally true. SPECIFICITY OF AMINOACYLATION Importance of Specificity Proof of the Adaptor Hypothesis, namely that when attached to tRNA, the amino acid no longer has any effect on codon selection, has long been available ~cited in ref. 2). The consequence of this fact is that AA-tRNA synthetases must be highly accurate both in their selection of an amino acid and of a tRNA, since any error in either recognition process will inevitably result in the incorporation of wrong amino acids into proteins.