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Information × Registration Number 0213U004870, 0110U004743 , R & D reports Title Molecular characteristics of tussuespecific protooncogene eEF1A2 and oncogene PTI-1 popup.stage_title Head Negrutskii B.S, Registration Date 26-12-2013 Organization Institute of Molecular Biology and Genetics of NASU popup.description2 The existence of two tissue-specific isoforms of eEF1A - eEF1A1 and eEF1A2 have shown for mammals. Two forms eEF1A encoded by different genes, but the proteins identity is 93 % and homology is 98 % . Protein eEF1A1 - expressed in most tissues, eEF1A2 replaces it in the nervous and muscular tissues in the development process. It is important that in spite of the great similarity of the primary structure, these isoforms are different in some of its features and functions as in the translation process, as well as in others. We have determined that the only isoform A1 forms a complex with calmodulin retaining predicted interaction sites. Thus, domains II and III isoform A1 of elongation translation factor able to interact with calmodulin . Physiological significance specific to interactions with A1 kalmodulin may lie in the fact that A2 isoform normally present only in nerve and muscle tissues , which , in turn , contain a large amount of calmodulin . It is possible that A2 in these tissues is necessary to avoid interaction with calmodulin, to ensure compliance canonical function of this protein in biosynthesis . The ability of different isoforms of A1 and A2 to interact with calcium - binding protein S100A1 and protein - chaperone Sgt1 is defined. Based on the results, different ability to interact with certain partners may explain the tumorigenicity isoform A2 unlike isoform A1 is proposed.5481 Product Description popup.authors Висловух А.А Власенко Д.О Новосильна О.В Порубльова Л.В Тросюк Т.В. Шалак В.Ф. popup.nrat_date 2020-04-02 Close