ArticleNucleic acids research2023
Global profiling of ribosomal protein acetylation reveals essentiality of acetylation homeostasis in maintaining ribosome assembly and function.
Article in Nucleic acids research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
- Translational control of Toxoplasma gondii differentiation.Bioscience reports · 2026Review
- Ribosome Biogenesis and Translational Control in Skeletal Muscle Atrophy and Hypertrophy: Mechanisms and Therapeutic Perspectives.Biomolecules · 2026Review
- Atlas of lysine acetylation in the mouse.bioRxiv : the preprint server for biology · 2026Article
- Bacterial ribosome heterogeneity facilitates rapid response to stress.Journal of bacteriology · 2025Review
- RPL35A Downregulation Suppresses Hepatocellular Carcinoma Cell Proliferation via NCAPG2 Inactivation.Cancer medicine · 2025Article
- Built differently or defective: can RNA exosomopathies cause ribosome heterogeneity?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Review
- Mechanisms of antibiofilm compounds JG-1 and M4 across multiple species: alterations of protein interactions essential to biofilm formation.Frontiers in cellular and infection microbiology · 2025Article
- Guided tour through the small protein landscape ofmicroLife · 2025Article
- circSORBS1 inhibits lung cancer progression by sponging miR-6779-5p and directly binding RUFY3 mRNA.Journal of translational medicine · 2024Article
- Bacterial protein acetylation: mechanisms, functions, and methods for study.Frontiers in cellular and infection microbiology · 2024Review
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Acetylation is a global post-translational modification that regulates various cellular processes. Bacterial acetylomic studies have revealed extensive acetylation of ribosomal proteins. However, the role of acetylation in regulating ribosome function remains poorly understood. In this study, we systematically profiled ribosomal protein acetylation and identified a total of 289 acetylated lysine residues in 52 ribosomal proteins (r-proteins) from Salmonella Typhimurium. The majority of acetylated lysine residues of r-proteins were found to be regulated by both acetyltransferase Pat and metabolic intermediate acetyl phosphate. Our results show that acetylation plays a critical role in the assembly of the mature 70S ribosome complex by modulating r-proteins binding to rRNA. Moreover, appropriate acetylation is important for the interactions between elongation factors and polysomes, as well as regulating ribosome translation efficiency and fidelity. Dysregulation of acetylation could alter bacterial sensitivity to ribosome-targeting antibiotics. Collectively, our data suggest that the acetylation homeostasis of ribosomes is crucial for their assembly and function. Furthermore, this mechanism may represent a universal response to environmental signals across different cell types.
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