Evidence for the formation of an unusual ternary complex of rabbit liver EF‐1α with GDP and deacylated tRNA

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Abstract
Eukaryotic translation elongation factor 1α is known to interact in GTP‐bound form with aminoacyl‐tRNA promoting its binding to the ribosome. In this paper another ternary complex [EF‐1α*GDP*deacylated tRNA], never considered in widely accepted elongation schemes, is reported for the first time. The formation of this unusual complex, postulated earlier (FEBS Lett. (1996) 382, 18–20), has been detected by four independent methods. [EF‐1α*GDP]‐interacting sites are located in the acceptor stem, TψC stem and TψC loop of tRNAPhe and tRNALeu molecules. Both tRNA and EF‐1α are found to undergo certain conformational changes during their interaction. The ability of EF‐1α to form a complex with deacylated tRNA indicates that the factor may perform an important role in tRNA and aminoacyl‐tRNA channeling in higher eukaryotic cells.