Oxidation of translation factor EF-G transiently retards the translational elongation cycle in Escherichia coli

Journal of Biochemistry
Takanori NaganoYoshitaka Nishiyama

Abstract

In Escherichia coli, elongation factor G (EF-G), a key protein in translational elongation, is particularly susceptible to oxidation. We demonstrated previously that EF-G is inactivated upon formation of an intramolecular disulphide bond. However, the details of the mechanism by which the oxidation of EF-G inhibits the function of EF-G on the ribosome remain to be elucidated. When we oxidized EF-G with hydrogen peroxide, neither the insertion of EF-G into the ribosome nor single-cycle translocation activity in vitro was affected. However, the GTPase activity and the dissociation of EF-G from the ribosome were suppressed when EF-G was oxidized. The synthesis of longer peptides was suppressed to a greater extent than that of a shorter peptide when EF-G was oxidized. Thus, the formation of the disulphide bond in EF-G might interfere with the hydrolysis of GTP that is coupled with dissociation of EF-G from the ribosome and might thereby retard the turnover of EF-G within the translational machinery. When we added thioredoxin to the suppressed translation system that included oxidized EF-G, translational activity was almost immediately restored. We propose that oxidation of EF-G might provide a regulatory mechanism for transient and...Continue Reading

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Jul 10, 2012·The Journal of Biological Chemistry·Takanori NaganoYoshitaka Nishiyama

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Citations

Dec 27, 2015·Trends in Plant Science·Marten MooreKarl-Josef Dietz
Sep 25, 2017·The Journal of Biological Chemistry·Daniel ShedlovskiyNatalia Shcherbik
Jan 21, 2016·The Journal of Biological Chemistry·Rayakorn YutthanasirikulYoshitaka Nishiyama
Nov 7, 2019·Cells·Natalia Shcherbik, Dimitri G Pestov
May 28, 2021·Frontiers in Molecular Biosciences·Michel Fasnacht, Norbert Polacek

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