{Reference Type}: Journal Article
{Title}: Ribosomal protein S18 acetyltransferase RimI is responsible for the acetylation of elongation factor Tu.
{Author}: Pletnev PI;Shulenina O;Evfratov S;Treshin V;Subach MF;Serebryakova MV;Osterman IA;Paleskava A;Bogdanov AA;Dontsova OA;Konevega AL;Sergiev PV;
{Journal}: J Biol Chem
{Volume}: 298
{Issue}: 5
{Year}: 05 2022
暂无{DOI}: 10.1016/j.jbc.2022.101914
{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.