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 tRNA Phe and tRNA Leu 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.
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