ArticleJournal of bacteriology2014
Essentiality of DevR/DosR interaction with SigA for the dormancy survival program in Mycobacterium tuberculosis.
Article in Journal of bacteriology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 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
23 citing papers in PubMed, 53 citations in OpenAlex.
- Molecular basis of DosR-dependent transcription activation in Mycobacterium tuberculosis.Nature communications · 2026Article
- Serine/threonine protein kinase phosphorylation of DosR alters target gene transcription mechanics and regulates Mycobacterium tuberculosis response to nitric oxide stress.PLoS genetics · 2026Article
- Multiple input-multiple output (MIMO) designs in two-component signalling systems of Mycobacterium tuberculosis.FEMS microbiology reviews · 2026Review
- Facile metabolic reprogramming distinguishes mycobacterial adaptation to hypoxia and starvation: ketosis drives starvation-induced persistence in M. bovis BCG.Communications biology · 2024Article
- Lsr2, a pleiotropic regulator at the core of the infectious strategy ofMicrobiology spectrum · 2024Article
- Metabolic Rewiring ofMetabolites · 2024Review
- Expanding the search for small-molecule antibacterials by multidimensional profiling.Nature chemical biology · 2022Review
- Exposure ofAntibiotics (Basel, Switzerland) · 2020Article
- Mechanisms of Drug-Induced Tolerance in Mycobacterium tuberculosis.Clinical microbiology reviews · 2020Review
- Metabolic Switching ofJournal of bacteriology · 2020Article
- Article
- Interplay of PhoP and DevR response regulators defines expression of the dormancy regulon in virulentThe Journal of biological chemistry · 2018Article
- Acetylation of lysine 182 inhibits the ability of Mycobacterium tuberculosis DosR to bind DNA and regulate gene expression during hypoxia.Emerging microbes & infections · 2018Article
- New Insights in to the Intrinsic and Acquired Drug Resistance Mechanisms in Mycobacteria.Frontiers in microbiology · 2017Review
- Expression, maturation and turnover of DrrS, an unusually stable, DosR regulated small RNA in Mycobacterium tuberculosis.PloS one · 2017Article
- Mycobacterium tuberculosis Transcription Machinery: Ready To Respond to Host Attacks.Journal of bacteriology · 2016Review
- Article
- DosS Is required for the complete virulence of mycobacterium tuberculosis in mice with classical granulomatous lesions.American journal of respiratory cell and molecular biology · 2015Article
- Article
- Molecular dissection of Mycobacterium tuberculosis integration host factor reveals novel insights into the mode of DNA binding and nucleoid compaction.The Journal of biological chemistry · 2014Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The DevR/DosR regulator is believed to play a key role in dormancy adaptation mechanisms of Mycobacterium tuberculosis in response to a multitude of gaseous stresses, including hypoxia, which prevails within granulomas. DevR activates transcription by binding to target promoters containing a minimum of two binding sites. The proximal site overlaps with the SigA -35 element, suggesting that DevR-SigA interaction is required for activating transcription. We evaluated the roles of 14 charged residues of DevR in transcriptional activation under hypoxic stress. Seven of the 14 alanine substitution mutants were defective in regulon activation, of which K191A, R197A, and K179A+K168A (designated K179A*) mutants were significantly or completely compromised in DNA binding. Four mutants, namely, E154A, R155A, E178A, and K208A, were activation defective in spite of binding to DNA and were classified as positive-control (pc) mutants. The SigA interaction defect of the E154A and E178A proteins was established by in vitro and in vivo assays and implies that these substitutions lead to an activation defect because they disrupt an interaction(s) with SigA. The relevance of DevR interaction to the transcriptional machinery was further established by the hypoxia survival phenotype displayed by SigA interaction-defective mutants. Our findings demonstrate the role of DevR-SigA interaction in the activation mechanism and in bacterial survival under hypoxia and establish the housekeeping sigma factor SigA as a molecular target of DevR. The interaction of DevR and RNA polymerase suggests a new and novel interceptable molecular interface for future antidormancy strategies for Mycobacterium tuberculosis.
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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.