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Information × Registration Number 0212U000545, 0109U005586 , R & D reports Title The structural and organization of translation apparatus in the cytoplasm of human cells popup.stage_title Head Negrutskii B.S, Registration Date 17-02-2012 Organization Institute of Molecular Biology and Genetics of NASU popup.description2 Abilities of initiation and elongation factors of different origin to form non-canonical complexes with deacylated tRNAs of different specificities and aminoacyl-tRNA synthetases were proved. We have shown that GDP forms of both eEF1A1 and eEF1A2 isoforms were able to interact with tRNAs specific for 9 amino acids. The formation of eEF1A*GDP*tRNA complexes were shown for yeast system as well for tRNA of three amino-acid specificities. Mutational affinity analysis of the complexes of three recombinant tRNA3Lys with eEF1A showed that changes in acceptor and T-stems of tRNA cause insignificant alterations in affinities, mostly for eEF1A2. For the first time we showed the formation of quaternary complex [eEF1A*GDP*тРНКSer*SerRS] and stabilizing effect of eEF1A*GDP in complex [eEF1A*GDP*tRNATyr*TyrRS]. For the first time we showed that eEF1A is able to interact with calmodulin. Possible functional role of such interaction is deciphered, which could be the promoting of competition with deacvylated tRNA for eEF1A*GDP. We have obtained crystals of eEF1A2 isoform with good difraction ability, which will be used to reveal spatial structure of mamamalian elongation factor 1A. Product Description popup.authors Бояршин К.С Веремєва М.В. Висловух А.А. Власенко Д.І. Гудзера О.Й. Коваленко М.І. Коваленко О.П. Крикливий І.А. Лукаш Т.О. Лукяненко Г.І Ляшенко І.А Новосильна О.В. Тукало М.А Футерник П.В. Шалак В.Ф. Яремчук Г.Д. popup.nrat_date 2020-04-02 Close