Search academic texts

Information × Registration Number 0215U008229, 0110U000693 , R & D reports Title Investigation of multiprotein translational nanocomplexes and their components popup.stage_title Head Negrutskii B. S., Доктор біологічних наук Registration Date 22-12-2015 Organization Institute of Molecular Biology and Genetics of NASU popup.description2 Protein biosynthesis in higher eukaryotes is the multikomponent process, which is attended by a few large groups are physically connected to each other, including the aminoacyl-tRNA synthetase complex MARS and the elongation factors complex eEF1A. We were found that the rate of diffusion of the aminoacyl-tRNA synthetases in the living cell is significantly delayed compared to the protein GFP and depends on an intact actin cytoskeleton, and the interaction with the ribosome, which is the first evidence for compartmentalization of the translational machinery obtained in living cells. It was shown that the lack of coordination changes in the number of different subunits of the translational complex eEF1B in human cancers at both the mRNA and protein level is the first evidence of the existence in the human tissues free from the complex subunits eEF1B and indicates a possible regulatory role of the individual subunits eEF1B in carcinogenesis. It was shown that the content of subunits eEF1H increased more than twice in 72% cardioesophageal tumor and 52% of the lung carcinomas, and remains unchanged in the renal carcinoma, which evidenced a certain specificity of these changes. For the first time it was revealed a violations in the eEF1A methylation in tumor tissues and identified lysine residues in the molecule eEF1A, methylation of which were changed. It was hypothesized that the change in the level of methylation of these residues could affect the interaction eEF1A with specific partner proteins in tumor cells what may be a mechanism of manifestation of eEF1A oncogenic function. For the first time it was demonstrated a difference for the ability of isoforms eEF1A1 i eEF1A2 to the formation of dimers, moreover the spatial structure of eEF1A1 dimers is a less compact than dimers of oncogenic isoforms eEF1A2. It was shown that only eEF1A1 is able to interact with signaling proteins calmodulin in a calcium-dependent fashion and localized a binding site. It was proven that calmodulin and tRNA compete for binding to eEF1A1, which opens up new possibilities regulatory calcium-mediated metabolic control of broadcasting. The data that both isoforms eEF1A are able to interact differently with actin filaments to form twists was obtained. It was shown that calmodulin prevents eEF1A1 to twist an actin filaments, which can be an additional mechanism for the participation of calcium in the regulation of the actin cytoskeleton. It was developed the procedures for obtaining preparative amounts of subunits eEF1Ba, eEF1Bb i eEF1Bg of translation factor eEF1B. We were obtained an evidence to suggest that all the subunits of this complex is nonglobular proteins and demonstrate an elongated shape in the solution. It was renovated eEF1B complex and its mini-complexes eEF1Ba * eEF1Bg and eEF1Bb * eEF1Bg in vitro Product Description popup.authors Вісловух А.А. Веремєва М. В. Власенко Д. І. Гавриленко С. С. Капустян Л. М. Коваленко М. І Новосильна О. В. Порубльова Л В Тросюк Т. В. Шалак В Ф popup.nrat_date 2020-04-02 Close