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Aim. The work is aimed at confirmation of earlier assumed mechanism of tRNA channeling. Methods. The methods of band shift assay and Forsters resonance energy transfer were used. Results. The affinities of mammalian tRNAs for two tissue specific isoforms of elongator factor eEF1A1 and eEF1A2 were compared. For the first time we have shown the ability of yeast eEF1A*GDP to form non-canonical ternary complex with deacylated tRNAs. The complexation of eukaryotic eEF1A with initiator tRNA, of both bacterial and mammalian origin, was also demonstrated. Conclusions. The formation of the non-canonical complexes of eEF1A*GDP with deacylated tRNAs is common for higher and lower eukaryotes, which is in favor of universality of eukaryotic tRNA-channelin

Interaction of different tRNAs with translation elongation factors 1A from lower and higher eukaryotes