ArticleNucleic acids research2013
Mechanism of DNA organization by Mycobacterium tuberculosis protein Lsr2.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
- Molecular Kaleidoscope of Nucleoid-Associated Proteins Regulatory Network and Chromosome Architecture in Mycobacterium Tuberculosis.Current microbiology · 2026Review
- Sequence-dependent co-condensation of Lsr2 with DNA elucidates the mechanism of genome compaction in Mycobacterium tuberculosis.Nucleic acids research · 2026Article
- NapR, a novel nucleoid-associated protein, regulates antioxidant defense in mycobacteria.mSphere · 2025Article
- Pore-C sequencing identifies episome-driven chromosome conformation perturbations differentiating pneumococcal epigenetic variants.PLoS pathogens · 2025Article
- Rok from B. subtilis: Bridging genome structure and transcription regulation.Molecular microbiology · 2025Review
- Zafirlukast induces DNA condensation and has bactericidal effect on replicatingAntimicrobial agents and chemotherapy · 2024Article
- Molecular and thermodynamic determinants of self-assembly and hetero-oligomerization in the enterobacterial thermo-osmo-regulatory protein H-NS.Nucleic acids research · 2024Article
- The B. subtilis Rok protein is an atypical H-NS-like protein irresponsive to physico-chemical cues.Nucleic acids research · 2022Article
- Novel anti-repression mechanism of H-NS proteins by a phage protein.Nucleic acids research · 2021Article
- Xenogeneic Silencing and Bacterial Genome Evolution: Mechanisms for DNA Recognition Imply Multifaceted Roles of Xenogeneic Silencers.Molecular biology and evolution · 2021Review
- Dynamics of the compartmentalized Streptomyces chromosome during metabolic differentiation.Nature communications · 2021Article
- Lsr2, a nucleoid-associated protein influencing mycobacterial cell cycle.Scientific reports · 2021Article
- The architects of bacterial DNA bridges: a structurally and functionally conserved family of proteins.Open biology · 2019Article
- Impact of Xenogeneic Silencing on Phage-Host Interactions.Journal of molecular biology · 2019Review
- Lsr2 Is an Important Determinant of Intracellular Growth and Virulence inFrontiers in microbiology · 2019Article
- A single molecule analysis of H-NS uncouples DNA binding affinity from DNA specificity.Nucleic acids research · 2018Article
- Transfer-matrix calculations of the effects of tension and torque constraints on DNA-protein interactions.Nucleic acids research · 2018Article
- Dimerization site 2 of the bacterial DNA-binding protein H-NS is required for gene silencing and stiffened nucleoprotein filament formation.The Journal of biological chemistry · 2018Article
- Regulation of the CRISPR-Associated Genes by Rv2837c (CnpB) via an Orn-Like Activity in Tuberculosis Complex Mycobacteria.Journal of bacteriology · 2018Article
- Interfering With DNA Decondensation as a Strategy Against Mycobacteria.Frontiers in microbiology · 2018Article
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Authors and funding
5 authors.
Funding
Abstract
Bacterial nucleoid-associated proteins, such as H-NS-like proteins in Enterobacteriaceae, are abundant DNA-binding proteins that function in chromosomal DNA organization and gene transcription regulation. The Mycobacterium tuberculosis Lsr2 protein has been proposed to be the first identified H-NS analogue in Gram-positive bacteria based on its capability to complement numerous in vivo functions of H-NS. Here, we report that Lsr2 cooperatively binds to DNA forming a rigid Lsr2 nucleoprotein complex that restricts DNA accessibility, similar to H-NS. On large DNA, the rigid Lsr2 nucleoprotein complexes can mediate DNA condensation into highly compact DNA conformations. In addition, the responses of Lsr2 nucleoprotein complex to environmental factors (salt concentration, temperature and pH) were studied over physiological ranges. These results provide mechanistic insights into how Lsr2 may mediate its gene silencing, genomic DNA protection and organization functions in vivo. Finally, our results strongly support that Lsr2 is an H-NS-like protein in Gram-positive bacteria from a structural perspective.
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