Biopolym. Cell. 2013; 29(3):177-187.
Specific features of protein biosynthesis in higher eukaryotes
1El'skaya A. V., 1Negrutskii B. S., 1Shalak V. F., 1Vislovukh A. A., 1Vlasenko D. O., 1Novosylna A. V., 1Lukash T. O., 1Veremieva M. V.
  1. Institute of Molecular Biology and Genetics, NAS of Ukraine
    150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680


Over 40 years of studies in the field of higher eukaryotic translation are summarized in the review. Among the pioneer results obtained we should especially accentuate the following: i) discovery of the adaptation of tRNAs and aminoacyl-tRNA synthetases (ARSs) cellular pools to the synthesis of specific proteins and modulation of the elongation rate by rare isoacceptor tRNAs; ii) the chaperone-like properties of the translation components (ribosomes and elongation factor eEF1A); characterization of high molecular weight complexes of ARSs; iii) functional compartmentalization, including channeling of tRNA in eukaryotic cells; iv) molecular mechanisms of channeling mediated by different non-canonical complexes involving eEF1A, tRNA and aminoacyl-tRNA synthetases; v) characterization of the crystal structure of eEF1A2; vi) comparison of spatial structure, molecular dynamics, tyrosine phosphorylation and abilities to interact with different protein partners of the eEF1A1 and eEF1A2 isoforms; vii) discovery of the microRNA-mediated control of the expression of the proto-oncogenic eEF1A2 isoform in cancer cells; viii) examination of the cancer-related changes in translation elongation complex eEF1H and mechanisms of oncogene PTI-1 action; ix) discovery of the third tRNA binding site on mammals ribosomes and the allosteric interaction of the 80S ribosomal A and E sites.
Keywords: protein biosynthesis, tRNA, aminoacyl-tRNA synthetases, eEF1A, eEF1H, РТІ-1


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