ArticleNucleic acids research2014
Direct regulation of topoisomerase activity by a nucleoid-associated protein.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
27 citing papers in PubMed, 50 citations in OpenAlex.
- Nucleoid-associated protein HU constrains transcription elongation to influence cellular functions, virulence, and drug tolerance in Mycobacterium tuberculosis.Nucleic acids research · 2026Article
- Nucleoid-associated proteins: molecular mechanisms in microbial adaptation.World journal of microbiology & biotechnology · 2025Review
- Bacterial chromatin proteins, transcription, and DNA topology: Inseparable partners in the control of gene expression.Molecular microbiology · 2024Review
- Variation of Structure and Cellular Functions of Type IA Topoisomerases across the Tree of Life.Cells · 2024Review
- StaR Is a Positive Regulator of Topoisomerase I Activity Involved in Supercoiling Maintenance inInternational journal of molecular sciences · 2023Article
- Enhanced binding of an HU homologue under increased DNA supercoiling preserves chromosome organisation and sustains Streptomyces hyphal growth.Nucleic acids research · 2022Article
- Nucleoid-associated proteins shape chromatin structure and transcriptional regulation across the bacterial kingdom.Transcription · 2021Review
- Bacterial transcription during growth arrest.Transcription · 2021Review
- Compaction and control-the role of chromosome-organizing proteins in Streptomyces.FEMS microbiology reviews · 2020Review
- Chromosome organization in bacteria: mechanistic insights into genome structure and function.Nature reviews. Genetics · 2020Review
- A highly processive actinobacterial topoisomerase I - thoughts onMicrobiology (Reading, England) · 2020Review
- Nucleoid Associated Proteins: The Small Organizers That Help to Cope With Stress.Frontiers in microbiology · 2020Review
- Transcription of Bacterial Chromatin.Journal of molecular biology · 2019Review
- An Update on African Swine Fever Virology.Viruses · 2019Review
- Genome-wide mapping of Topoisomerase I activity sites reveal its role in chromosome segregation.Nucleic acids research · 2019Article
- Transcriptional Response ofFrontiers in microbiology · 2019Article
- G-Quadruplex-Forming DNA Aptamers Inhibit the DNA-Binding Function of HupB and Mycobacterium tuberculosis Entry into Host Cells.Molecular therapy. Nucleic acids · 2018Article
- The Origin of Chromosomal Replication Is Asymmetrically Positioned on the Mycobacterial Nucleoid, and the Timing of Its Firing Depends on HupB.Journal of bacteriology · 2018Article
- Acetylation by Eis and Deacetylation by Rv1151c of Mycobacterium tuberculosis HupB: Biochemical and Structural Insight.Biochemistry · 2018Article
- Boldine-Derived Alkaloids Inhibit the Activity of DNA Topoisomerase I and Growth ofFrontiers in microbiology · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The topological homeostasis of bacterial chromosomes is maintained by the balance between compaction and the topological organization of genomes. Two classes of proteins play major roles in chromosome organization: the nucleoid-associated proteins (NAPs) and topoisomerases. The NAPs bind DNA to compact the chromosome, whereas topoisomerases catalytically remove or introduce supercoils into the genome. We demonstrate that HU, a major NAP of Mycobacterium tuberculosis specifically stimulates the DNA relaxation ability of mycobacterial topoisomerase I (TopoI) at lower concentrations but interferes at higher concentrations. A direct physical interaction between M. tuberculosis HU (MtHU) and TopoI is necessary for enhancing enzyme activity both in vitro and in vivo. The interaction is between the amino terminal domain of MtHU and the carboxyl terminal domain of TopoI. Binding of MtHU did not affect the two catalytic trans-esterification steps but enhanced the DNA strand passage, requisite for the completion of DNA relaxation, a new mechanism for the regulation of topoisomerase activity. An interaction-deficient mutant of MtHU was compromised in enhancing the strand passage activity. The species-specific physical and functional cooperation between MtHU and TopoI may be the key to achieve the DNA relaxation levels needed to maintain the optimal superhelical density of mycobacterial genomes.
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Registered trials
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.