ArticleThe Journal of biological chemistry2022
Ribosomal protein S18 acetyltransferase RimI is responsible for the acetylation of elongation factor Tu.
Article in The Journal of biological chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 18 citations in OpenAlex.
- A jumbo cyanophage encodes the most comprehensive ribosomal protein set in the known virosphere.The ISME journal · 2026Article
- NProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Characterization of Probiotic Properties and Whole-Genome Analysis ofMicroorganisms · 2024Article
- Whole genome sequencing distinguishes skin colonizing from infection-associatedFrontiers in cellular and infection microbiology · 2024Article
- Multi-omics Data Reveal the Effect of Sodium Butyrate on Gene Expression and Protein Modification in Streptomyces.Genomics, proteomics & bioinformatics · 2023Article
- Global profiling of ribosomal protein acetylation reveals essentiality of acetylation homeostasis in maintaining ribosome assembly and function.Nucleic acids research · 2023Article
- Morphological and physiological adaptations of psychrophilic Pseudarthrobacter psychrotolerans YJ56 under temperature stress.Scientific reports · 2023Article
- Article
- Insights into the molecular mechanism of translation inhibition by the ribosome-targeting antibiotic thermorubin.Nucleic acids research · 2023Article
- Genomic alterations involved in fluoroquinolone resistance development in Staphylococcus aureus.PloS one · 2023Article
- Evolutionary Conserved Short Linear Motifs Provide Insights into the Cellular Response to Stress.Antioxidants (Basel, Switzerland) · 2022Article
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Authors and funding
12 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
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.
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