Specific features of protein biosynthesis in higher eukaryotes

• Дата: 2013
• Автори: El'skaya, A.V., Negrutskii, B.S., Shalak, V.F., Vislovukh, A.A., Vlasenko, D.O., Novosylna, A.V., Lukash, T.O., Veremieva, M.V.
• Формат: Стаття
• Мова: English
• Опубліковано: Інститут молекулярної біології і генетики НАН України 2013
• Назва видання: Вiopolymers and Cell
• Теми: Reviews
• Онлайн доступ: http://dspace.nbuv.gov.ua/handle/123456789/152573
• Назва журналу: Digital Library of Periodicals of National Academy of Sciences of Ukraine
• Цитувати: Specific features of protein biosynthesis in higher eukaryotes / A.V. El'skaya, B.S. Negrutskii, V.F. Shalak, A.A. Vislovukh, D.O. Vlasenko, A.V. Novosylna, T.O. Lukash, M.V. Veremieva // Вiopolymers and Cell. — 2013. — Т. 29, №. 3. — С. 177-187. — Бібліогр.: 60 назв. — англ.

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.