ArticleThe EMBO journal2018
Histone methyltransferase SUV39H1 participates in host defense by methylating mycobacterial histone-like protein HupB.
Article in The EMBO journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Nucleoid-associated protein HU constrains transcription elongation to influence cellular functions, virulence, and drug tolerance in Mycobacterium tuberculosis.Nucleic acids research · 2026Article
- Epigenetic modulation in tuberculosis - mycobacterial defense mechanism to host immune responses.Frontiers in immunology · 2026Review
- A machine learning model and molecular clusters of epigenetic chromatin regulators in tuberculosis based on bioinformatics and clinical samples.Scientific reports · 2025Article
- The pathway of autophagy in the epigenetic landscape ofAutophagy · 2025Review
- Increased autophagy activity regulated by LC3B gene promoter DNA methylation is associated with progression to active pulmonary tuberculosis disease.Respiratory research · 2025Article
- The activity of CobB1 protein deacetylase contributes to nucleoid compaction in Streptomyces venezuelae spores by increasing HupS affinity for DNA.Nucleic acids research · 2024Article
- SUV39H1-driven NFATc1 methylation is essential for the c-Cbl-mediated degradation of NFATc1 in an osteoclast lineage.Genes & diseases · 2024Article
- Article
- Epigenetic landscape of intestinal cell line HT29 cocultured withEpigenomics · 2024Article
- Loss of H3K9 trimethylation alters chromosome compaction and transcription factor retention during mitosis.Nature structural & molecular biology · 2023Article
- Host-directed therapy against tuberculosis: Concept and recent developments.Journal of biosciences · 2023Review
- Article
- HupB, a nucleoid-associated protein, is critical for survival ofFrontiers in microbiology · 2022Article
- Structure, Activity and Function of the Suv39h1 and Suv39h2 Protein Lysine Methyltransferases.Life (Basel, Switzerland) · 2021Review
- Iron uptake and transport by the carboxymycobactin-mycobactin siderophore machinery of Mycobacterium tuberculosis is dependent on the iron-regulated protein HupB.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2021Article
- Methylation of two-component response regulator MtrA in mycobacteria negatively modulates its DNA binding and transcriptional activation.The Biochemical journal · 2020Article
- Transcriptional portrait of M. bovis BCG during biofilm production shows genes differentially expressed during intercellular aggregation and substrate attachment.Scientific reports · 2020Article
- Involvement of Transcription Elongation Factor GreA inFrontiers in microbiology · 2020Article
- Substrate recognition by theThe Journal of biological chemistry · 2019Article
- Moonlighting activity of the epigenetic machinery restrains infection.The EMBO journal · 2018Article
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4 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Host cell defense against an invading pathogen depends upon various multifactorial mechanisms, several of which remain undiscovered. Here, we report a novel defense mechanism against mycobacterial infection that utilizes the histone methyltransferase, SUV39H1. Normally, a part of the host chromatin, SUV39H1, was also found to be associated with the mycobacterial bacilli during infection. Its binding to bacilli was accompanied by trimethylation of the mycobacterial histone-like protein, HupB, which in turn reduced the cell adhesion capability of the bacilli. Importantly, SUV39H1-mediated methylation of HupB reduced the mycobacterial survival inside the host cell. This was also true in mice infection experiments. In addition, the ability of mycobacteria to form biofilms, a survival strategy of the bacteria dependent upon cell-cell adhesion, was dramatically reduced in the presence of SUV39H1. Thus, this novel defense mechanism against mycobacteria represents a surrogate function of the epigenetic modulator, SUV39H1, and operates by interfering with their cell-cell adhesion ability.
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