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cDNA as well as amino acid sequencing has revealed the complete primary structure of elongation factor EF‐1 alpha from the brine shrimp Artemia. A comparison with the published sequences of bacterial EF‐Tu, mitochondrial EF‐Tu and chloroplastic EF‐Tu shows that distinct areas of these polypeptide chains are conserved in evolution. The evolutionary distance between prokaryotic and eukaryotic types of EF‐Tu is larger than among bacterial and organellar EF‐ Tus . A number of regions present in both EF‐Tu and EF‐G from Escherichia coli are also found in EF‐1 alpha from Artemia.

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In the course of a structural analysis of the a-chain of elongation factor 1 from Artemia sulina cysts, we present four amino acid sequences comprising together half of the polypeptide chain. A comparison of these sequences with the primary structure of elongation factor EF-Tu from Escherichia coli reveals a clear correspondence between the eukaryotic and prokaryotic protein throughout their polypeptide chains. The results support a basic conservation of the structure of the aminoacyl-tRNA carrying enzyme in evolution.The occurrence, in the eukaryotic factor, of several c-trimethyllysine residues, is remarkable.

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