ArticleNucleic acids research2024
Lysine acetylation regulates the AT-rich DNA possession ability of H-NS.
Article in Nucleic acids research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- First Lysine Lactylation Profiling inMicroorganisms · 2026Article
- PLysPTM-HGNN: predicting lysine PTM sites of proteins using hybrid graph neural networks.BMC bioinformatics · 2026Article
- MarA binds and activates the ABC efflux pump YadGH to confer conditional macrolide resistance in AcrB-deficientFrontiers in microbiology · 2026Article
- Post-translational modifications of the nucleoid protein H-NS: sites, mechanisms, and regulatory cues.FEMS microbiology reviews · 2025Review
- The Negative Regulatory Role of Transcriptional Regulator H-NS on the Type VI Secretion System inInfection and drug resistance · 2025Article
- Decoding the regulatory networks ofFrontiers in cellular and infection microbiology · 2025Article
- Unveiling the Role of β-Glucosidase Genes inInternational journal of molecular sciences · 2024Article
- Bacterial chromatin proteins, transcription, and DNA topology: Inseparable partners in the control of gene expression.Molecular microbiology · 2024Review
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Authors and funding
7 authors.
Funding
Abstract
H-NS, the histone-like nucleoid-structuring protein in bacteria, regulates the stability of the bacterial genome by inhibiting the transcription of horizontally transferred genes, such as the type III and type VI secretion systems (T3/T6SS). While eukaryotic histone posttranslational modifications (PTMs) have been extensively studied, little is known about prokaryotic H-NS PTMs. Here, we report that the acetylation of H-NS attenuates its ability to silence horizontally transferred genes in response to amino acid nutrition and immune metabolites. Moreover, LC-MS/MS profiling showed that the acetyllysine sites of H-NS and K120 are indispensable for its DNA-binding ability. Acetylation of K120 leads to a low binding affinity for DNA and enhances T3/T6SS expression. Furthermore, acetylation of K120 impairs the AT-rich DNA recognition ability of H-NS. In addition, lysine acetylation in H-NS modulates in vivo bacterial virulence. These findings reveal the mechanism underlying H-NS PTMs and propose a novel mechanism by which bacteria counteract the xenogeneic silencing of H-NS.
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