Specific features of protein biosynthesis in higher eukaryotes

Abstract

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

Mass spectrometry‐based proteomic analysis reveals the interacting partners of lipin1

“…Among these interacting proteins, for instance, eEF1A1 is an isoforms of eEF1A, which is one of ribosomal elongation complexes of the polypeptide elongation machinery in eukaryotic cells . Despite its main translation function, eEF1A is capable of interacting with numerous non‐translational proteins which are not directly related to protein biosynthesis.…”

Comparison of the ability of mammalian eEF1A1 and its oncogenic variant eEF1A2 to interact with actin and calmodulin

“…Translation elongation factor eEF1A plays a main role in ribosomal polypeptide synthesis while providing the delivery of aminoacyl-tRNAs to the ribosome A-site (Negrutskii and El'skaya, 1998;El'skaya et al, 2013). This protein has also been shown to be multifunctional and is known to be involved in a number of nontranslational cellular processes (Ejiri, 2002;Lamberti et al, 2004;Abbas et al, 2015).…”

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“…Two tissue specific isoforms of translation elongation factor 1A (eEF1A1 and eEF1A2), with mutually exclusive expression, provide efficient delivery and binding of aminoacyl-tRNA to 80S ribosomes [1]. eEF1A2 functions in neurons, myocytes, cardiomyocytes and some other highly specialized cells while eEF1A1 contributes to mRNA translation in all other tissues of Mammalia [2].…”