ArticleProceedings of the National Academy of Sciences of the United States of America2010
Lsr2 is a nucleoid-associated protein that targets AT-rich sequences and virulence genes in Mycobacterium tuberculosis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 130 papers.
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Who cites it
130 citing papers in PubMed, 227 citations in OpenAlex.
- Identifying Two New Ros/MucR Proteins: An Atypical Structure with a Divergent Function.Biomolecules · 2026Article
- Beyond Inhibition: Sublethal Rifampicin-Induced Molecular Adaptations Confer Phenotypic Drug Tolerance in Mycobacteria.ACS infectious diseases · 2026Article
- 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
- Structural Studies on the M. tuberculosis Nucleoid-associated-Protein, NapA, Indicates DNA Bridging Mechanism.Journal of molecular biology · 2025Article
- Decoding the role of DNA sequence on protein-DNA co-condensation.PLoS computational biology · 2025Article
- LsrL modulates Lsr2-induced chromatin structure to tune biosynthetic gene cluster regulation inbioRxiv : the preprint server for biology · 2025Article
- Breaking the silence-role of MucR as a virulence determinant inJournal of bacteriology · 2025Review
- The MarR family transcription factor SlyA senses iron and respiratory status in enteric bacteria.mBio · 2025Article
- Loss of the ESX-5 secretion locus inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Conserved Heterochromatin-like Structures with Local Regulators Mediate the Iron Stress Response in Mycobacteria.bioRxiv : the preprint server for biology · 2025Article
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- Emergence of linezolid-resistant Enterococcus cecorum clade F harboring optrA/fexA causing enterococcal spondylitis in commercial broilers in China.BMC microbiology · 2025Article
- Important Role of Bacterial Nucleoid-Associated Proteins in Discovery of Novel Secondary Metabolites.International journal of molecular sciences · 2025Review
- Artificial Intelligence-Enhanced Analysis of Genomic DNA Visualized with Nanoparticle-Tagged Peptides under Electron Microscopy.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
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- Rok from B. subtilis: Bridging genome structure and transcription regulation.Molecular microbiology · 2025Review
- Circular oligomeric particles formed by Ros/MucR family members mediate DNA organization in α-proteobacteria.Nucleic acids research · 2024Article
70 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
Bacterial nucleoid-associated proteins play important roles in chromosome organization and global gene regulation. We find that Lsr2 of Mycobacterium tuberculosis is a unique nucleoid-associated protein that binds AT-rich regions of the genome, including genomic islands acquired by horizontal gene transfer and regions encoding major virulence factors, such as the ESX secretion systems, the lipid virulence factors PDIM and PGL, and the PE/PPE families of antigenic proteins. Comparison of genome-wide binding data with expression data indicates that Lsr2 binding results in transcriptional repression. Domain-swapping experiments demonstrate that Lsr2 has an N-terminal dimerization domain and a C-terminal DNA-binding domain. Nuclear magnetic resonance analysis of the DNA-binding domain of Lsr2 and its interaction with DNA reveals a unique structure and a unique mechanism that enables Lsr2 to discriminately target AT-rich sequences through interactions with the minor groove of DNA. Taken together, we provide evidence that mycobacteria have employed a structurally distinct molecule with an apparently different DNA recognition mechanism to achieve a function similar to the Enterobacteriaceae H-NS, likely coordinating global gene regulation and virulence in this group of medically important bacteria.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.