Abstract
This work was supported by the interdisciplinary scientific program of the National Academy of Sciences of Ukraine “Fundamental basis for molecular and cell biotechnologies” (2010 2014).
Highlights
Guanine-nucleotide exchange factors (GEFs) play an important role during the elongation cycle of protein biosynthesis in eukaryotes catalyzing the GDP/ GTP exchange on translation elongation factor 1A and, restoring its active GTP bound conformation
The exchange on translation elongation factor 1A (eEF1A)*GTP molecules form the complexes with various aminoacylated tRNAs and deliver them to the ribosome ensuring the process of protein biosynthesis [1]
By multiple sequence alignment four conservative domains can be delineated in the primary structure of eEF1Bβ from different species (Fig. 1A): the N-terminal domain contains highly conservative and low conservative regions, the leucine-zipper motive [14, 15], the central acidic region [12] and the C-terminal domain responsible for GEF activity [7]
Summary
Guanine-nucleotide exchange factors (GEFs) play an important role during the elongation cycle of protein biosynthesis in eukaryotes catalyzing the GDP/ GTP exchange on translation elongation factor 1A (eEF1A) and, restoring its active GTP bound conformation. There are two isoforms of eEF1A (designated eEF1A1 and eEF1A2) that share 97 % amino acid homology but are encoded by different genes [2] Both eEF1A1 and eEF1A2 have different non-canonical functions, but their role in translation is believed to be identical [2,3,4]. GEFs that participate in translation elongation are organized in a stable macromolecular complex, eEF1B, containing three subunits designated eEF1Bα, eEF1Bβ and eEF1Bγ. We use the unifying nomenclature proposed by Merrick [5] Both eEF1Bα and eEF1Bβ catalyze the GDP/GTP exchange on eEF1A, while a functional role of eEF1Bγ is still poorly understood [3]. Deletion of the eEF1Bα N-terminal domain as well as formation of a tight complex with the eEF1Bγ N-terminal domain eliminated this inhibitory effect [9]
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