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A non‐catalytic N‐terminal domain negatively influences the nucleotide exchange activity of translation elongation factor 1Bα
Author(s) -
Trosiuk Tetiana V.,
Shalak Vyacheslav F.,
Szczepanowski Roman H.,
Negrutskii Boris S.,
El'skaya Anna V.
Publication year - 2016
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.13599
Subject(s) - guanine nucleotide exchange factor , elongation factor , biochemistry , eukaryotic translation , elongation , nucleotide , microbiology and biotechnology , chemistry , biology , translation (biology) , signal transduction , rna , materials science , ribosome , ultimate tensile strength , messenger rna , metallurgy , gene
Eukaryotic translation elongation factor 1Bα ( eEF 1Bα) is a functional homolog of the bacterial factor EF ‐Ts, and is a component of the macromolecular eEF 1B complex. eEF 1Bα functions as a catalyst of guanine nucleotide exchange on translation elongation factor 1A ( eEF 1A). The C‐terminal domain of eEF 1Bα is necessary and sufficient for its catalytic activity, whereas the N‐terminal domain interacts with eukaryotic translation elongation factor 1Bγ ( eEF 1Bγ) to form a tight complex. However, eEF 1Bγ has been shown to enhance the catalytic activity of eEF 1Bα attributed to the C‐terminal domain of eEF 1Bα. This suggests that the N‐terminal domain of eEF 1Bα may in some way influence the guanine nucleotide exchange process. We have shown that full‐length recombinant eEF 1Bα and its truncated forms are non‐globular proteins with elongated shapes. Truncation of the N‐terminal domain of eEF 1Bα, which is dispensable for catalytic activity, resulted in acceleration of the rate of guanine nucleotide exchange on eEF 1A compared to full‐length eEF 1Bα. A similar effect on the catalytic activity of eEF 1Bα was observed after its interaction with eEF 1Bγ. We suggest that the non‐catalytic N‐terminal domain of eEF 1Bα may interfere with eEF 1A binding to the C‐terminal catalytic domain, resulting in a decrease in the overall rate of the guanine nucleotide exchange reaction. Formation of a tight complex between the eEF 1Bγ and eEF 1Bα N‐terminal domains abolishes this inhibitory effect.