Ribosomal protein S18 acetyltransferase RimI is responsible for the acetylation of elongation factor Tu.

The Journal of biological chemistry 2022 May

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N-terminal acetylation is widespread in the eukaryotic proteome but in bacteria is restricted to a small number of proteins mainly involved in translation. It was long known that elongation factor Tu (EF-Tu) is N-terminally acetylated, whereas the enzyme responsible for this process was unclear. Here, we report that RimI acetyltransferase, known to modify ribosomal protein S18, is likewise responsible for N-acetylation of the EF-Tu. With the help of inducible tufA expression plasmid, we demonstrated that the acetylation does not alter the stability of EF-Tu. Binding of aminoacyl tRNA to the recombinant EF-Tu in vitro was found to be unaffected by the acetylation. At the same time, with the help of fast kinetics methods, we demonstrate that an acetylated variant of EF-Tu more efficiently accelerates A-site occupation by aminoacyl-tRNA, thus increasing the efficiency of in vitro translation. Finally, we show that a strain devoid of RimI has a reduced growth rate, expanded to an evolutionary timescale, and might potentially promote conservation of the acetylation mechanism of S18 and EF-Tu. This study increased our understanding of the modification of bacterial translation apparatus. Copyright © 2022 The Authors. Published by Elsevier Inc. All rights reserved.

Citation

Philipp I Pletnev, Olga Shulenina, Sergey Evfratov, Vsevolod Treshin, Maksim F Subach, Marina V Serebryakova, Ilya A Osterman, Alena Paleskava, Alexey A Bogdanov, Olga A Dontsova, Andrey L Konevega, Petr V Sergiev. Ribosomal protein S18 acetyltransferase RimI is responsible for the acetylation of elongation factor Tu. The Journal of biological chemistry. 2022 May;298(5):101914