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

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

    Research output: Contribution to journalArticlepeer-review

    Abstract

    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.

    Original languageEnglish
    Article number101914
    JournalJournal of Biological Chemistry
    Volume298
    Issue number5
    DOIs
    Publication statusPublished - 1 May 2022

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