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Most strains are naturally competent. Although some information is available about factors that enhance or reduce the frequency of the transformation of this bacterium, the regulatory elements and mechanisms are barely understood. In this article, we describe studies on the role of the histone-like nucleoid structuring protein, H-NS, in the regulation of the expression of genes related to natural competency and the ability to uptake foreign DNA. The expression levels of the natural transformation-related genes , , , , , , and significantly increased in a Δ derivative of A118. The complementation of the mutant with a recombinant plasmid harboring restored the expression levels of six of these genes ( remained expressed at high levels) to those of the wild-type strain. The transformation frequency of the A118 Δ strain was significantly higher than that of the wild-type. Similar, albeit not identical, there were consequences when was deleted from the hypervirulent AB5075 strain. In the AB5075 complemented strain, the reduction in gene expression in a few cases was not so pronounced that it reached wild-type levels, and the expression of was enhanced further. In conclusion, the expression of all seven transformation-related genes was enhanced after deleting in A118 and AB5075, and these modifications were accompanied by an increase in the cells' transformability. The results highlight a role of H-NS in natural competence.
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http://dx.doi.org/10.3390/pathogens10091083 | DOI Listing |
FEMS Microbiol Rev
September 2025
State Key Laboratory of Tropical Oceanography, South China Sea Institute of Oceanology, Chinese Academy of Sciences, Guangzhou 510301, China.
Histone-like nucleoid structuring protein H-NS plays a pivotal role in orchestrating bacterial chromatin and regulating horizontal gene transfer (HGT) elements. In response to environmental signals, H-NS undergoes dynamic post-translational modifications (PTMs) that resemble the epigenetic codes of eukaryotic histones. This review explores how environmental cues regulate PTMs at specific sites within distinct domains of H-NS, thereby modulating its oligomerization and DNA-binding capabilities to reprogram bacterial responses.
View Article and Find Full Text PDFPhilos Trans R Soc Lond B Biol Sci
September 2025
Department of Plant and Environmental Sciences, University of Copenhagen, DK-1871 Frederiksberg, Denmark.
CRISPR-Cas is an adaptive immune system of bacteria and archaea that protects against foreign genetic elements. In and , CRISPR-Cas is inhibited by the conserved global repressor the histone-like nucleoid structuring protein (H-NS), which blocks the expression of AT-rich horizontally acquired genes. While the opportunistic pathogen harbours two partially redundant H-NS homologues, MvaT and MvaU, their role in CRISPR-Cas regulation in this bacterium remains unexplored.
View Article and Find Full Text PDFNature
August 2025
Department of Biochemistry and Molecular Pharmacology, New York University Grossman School of Medicine, New York, NY, USA.
Unravelling how genomes are spatially organized and how their three-dimensional (3D) architecture drives cellular functions remains a major challenge in biology. In bacteria, genomic DNA is compacted into a highly ordered, condensed state called nucleoid. Despite progress in characterizing bacterial 3D genome architecture over recent decades, the fine structure and functional organization of the nucleoid remain elusive due to low-resolution contact maps from methods such as Hi-C.
View Article and Find Full Text PDFPathogens
June 2025
Department of Microbiology, University of Georgia, Athens, GA 30602, USA.
Here we report that the Typhimurium NatB (NatB) protein -terminal acetyltransferase acetylated the -terminal methionine of the nucleoid-associated HU proteins. Our findings were supported by an in vitro analysis of acetylation of the HUα and HUβ proteins and lysine-null (K-null) variants, and by an in vivo analysis of the effect of acetylation on HU-mediated transcriptional regulation of a known target of HU, the promoter. NatB did not acetylate the initiating methionines of HU proteins that were oxidized to methionine sulfoxide, but the reduction of these methionine sulfoxide residues restored the acetylation of HU proteins by NatB.
View Article and Find Full Text PDFInfect Drug Resist
June 2025
Department of Clinical Laboratory, the First Affiliated Hospital of Wenzhou Medical University; Key Laboratory of Clinical Laboratory Diagnosis and Translational Research of Zhejiang Province, Wenzhou, People's Republic of China.
Introduction: This study investigates the negative regulatory role of the global transcriptional regulator H-NS (Histone-like Nucleoid Structuring Protein) on the Type VI secretion system (T6SS) in (). We explored potential targets of H-NS mediated silencing or activation within the regulation of T6SS, along with the specific regulatory mechanisms involved, thereby providing a theoretical foundation for further research on invasive infections stemming from mixed infections and the development of therapeutic target.
Methods: Using the plasmids pAT04 and pYMAb2-hyg, we constructed ATCC19606 strains with the gene knocked out (ABΔ) and overexpressed (AB+).