ReviewJournal of microbiology (Seoul, Korea)2020
Regulation of gene expression by protein lysine acetylation in Salmonella.
Review in Journal of microbiology (Seoul, Korea), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Acetyl-Phosphate Dependent Protein Acetylation in Neisseria gonorrhoeae.MicrobiologyOpen · 2026Article
- Structural basis of the catalytic and allosteric mechanism of bacterial acetyltransferase PatZ.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Reversible acetylation of ribosomal protein S1 serves as a smart switch for Salmonella to rapidly adapt to host stress.Nucleic acids research · 2025Article
- Acetyl-proteome profiling revealed the role of lysine acetylation in erythromycin resistance ofHeliyon · 2024Article
- Lysine acetylation regulates the AT-rich DNA possession ability of H-NS.Nucleic acids research · 2024Article
- Acetylomics reveals an extensive acetylation diversity withinmicroLife · 2024Article
- Short-chain fatty acids in breast milk and their relationship with the infant gut microbiota.Frontiers in microbiology · 2024Article
- Bacterial protein acetylation: mechanisms, functions, and methods for study.Frontiers in cellular and infection microbiology · 2024Review
- Acetylation of K188 and K192 inhibits the DNA-binding ability of NarL to regulateApplied and environmental microbiology · 2023Article
- Pat- and Pta-mediated protein acetylation is required for horizontally-acquired virulence gene expression in Salmonella Typhimurium.Journal of microbiology (Seoul, Korea) · 2022Article
- Acetylation of CspC Controls the Las Quorum-Sensing System through Translational Regulation ofmBio · 2022Article
- Acetylome and Succinylome Profiling ofAntibiotics (Basel, Switzerland) · 2022Article
- Acetylation of the CspA family protein CspC controls the type III secretion system through translational regulation of exsA in Pseudomonas aeruginosa.Nucleic acids research · 2021Article
- Transcriptional Regulation of the Multiple Resistance Mechanisms inPathogens (Basel, Switzerland) · 2021Review
- Trans-acting regulators of ribonuclease activity.Journal of microbiology (Seoul, Korea) · 2021Review
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein lysine acetylation influences many physiological functions, such as gene regulation, metabolism, and disease in eukaryotes. Although little is known about the role of lysine acetylation in bacteria, several reports have proposed its importance in various cellular processes. Here, we discussed the function of the protein lysine acetylation and the post-translational modifications (PTMs) of histone-like proteins in bacteria focusing on Salmonella pathogenicity. The protein lysine residue in Salmonella is acetylated by the Pat-mediated enzymatic pathway or by the acetyl phosphate-mediated non-enzymatic pathway. In Salmonella, the acetylation of lysine 102 and lysine 201 on PhoP inhibits its protein activity and DNA-binding, respectively. Lysine acetylation of the transcriptional regulator, HilD, also inhibits pathogenic gene expression. Moreover, it has been reported that the protein acetylation patterns significantly differ in the drug-resistant and -sensitive Salmonella strains. In addition, nucleoid-associated proteins such as histone-like nucleoid structuring protein (H-NS) are critical for the gene silencing in bacteria, and PTMs in H-NS also affect the gene expression. In this review, we suggest that protein lysine acetylation and the post-translational modifications of H-NS are important factors in understanding the regulation of gene expression responsible for pathogenicity in Salmonella.
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