Quaternary Organization of the Human EEF1B Complex Reveals Unique Multi-GEF Domain Assembly

Overview

Journal Nucleic Acids Res

Publisher Oxford University Press

Specialty Biochemistry

Date 2022 Aug 16

PMID 35971611

Authors

Tetiana V Bondarchuk

Vyacheslav F Shalak

Dmytro M Lozhko

Agnieszka Fatalska

Roman H Szczepanowski

Vladyslava Liudkovska

Oleksandr Yu Tsuvariev

Michal Dadlez

Anna V Elskaya

Boris S Negrutskii

Affiliations

Soon will be listed here.

Abstract

Protein synthesis in eukaryotic cell is spatially and structurally compartmentalized that ensures high efficiency of this process. One of the distinctive features of higher eukaryotes is the existence of stable multi-protein complexes of aminoacyl-tRNA synthetases and translation elongation factors. Here, we report a quaternary organization of the human guanine-nucleotide exchange factor (GEF) complex, eEF1B, comprising α, β and γ subunits that specifically associate into a heterotrimeric form eEF1B(αβγ)3. As both the eEF1Bα and eEF1Bβ proteins have structurally conserved GEF domains, their total number within the complex is equal to six. Such, so far, unique structural assembly of the guanine-nucleotide exchange factors within a stable complex may be considered as a 'GEF hub' that ensures efficient maintenance of the translationally active GTP-bound conformation of eEF1A in higher eukaryotes.

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