Investigation of the complexes of elongation factor 1A with tRNASer and seryl-tRNA synthetase

Futernyk, P. V.; Pogribna, A. P.; Petrushenko, Z. M.; Negrutski, B. S.; El'skaya, G. V.

doi:10.7124/bc.000687

Biopolym. Cell. 2004; 20(1-2):17-23.

http://dx.doi.org/10.7124/bc.000687

Investigation of the complexes of elongation factor 1A with tRNA^Ser and seryl-tRNA synthetase

1Futernyk P. V., 1Pogribna A. P., 1Petrushenko Z. M., 1Negrutski B. S., 1El'skaya G. V.

Institute of Molecular Biology and Genetics, NAS of Ukraine
150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680

Abstract

To investigate the mechanism of tRNA channeling the formation of non-canonical complexes of elongation factor 1A1 with deacylated tRNA^Ser and seryl-tRNA synthetase was studied using band shift assay. The stability of these complexes was estimated. The formation of non-canonical complex of tRNA with the tissue-specific isoform of elongation factor 1A2 was examined and found to be more stable than the analogous complex with eEF1A1. Our results are in accordance with the proposed earlier mechanism of tRNA channeling during the elongation cycle of protein biosynthesis.

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