ArticleJournal of bacteriology2010
Different roles of DosS and DosT in the hypoxic adaptation of Mycobacteria.
Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
33 citing papers in PubMed, 59 citations in OpenAlex.
- Molecular basis of DosR-dependent transcription activation in Mycobacterium tuberculosis.Nature communications · 2026Article
- Multiple input-multiple output (MIMO) designs in two-component signalling systems of Mycobacterium tuberculosis.FEMS microbiology reviews · 2026Review
- Exploring the Protein Landscape of Dormant Mycobacterium tuberculosis Through In Vitro Functional Studies.Advances in experimental medicine and biology · 2026Review
- Inactivation of cAMP receptor protein (MSMEG_6189) increases isoniazid susceptibility inJournal of bacteriology · 2025Article
- Oxygen affinities of DosT and DosS sensor kinases with implications for hypoxia adaptation in Mycobacterium tuberculosis.Journal of inorganic biochemistry · 2024Article
- Mycobacterial biofilms: A therapeutic target against bacterial persistence and generation of antibiotic resistance.Heliyon · 2024Review
- Rel-dependent decrease in the expression of ribosomal protein genes by inhibition of the respiratory electron transport chain inFrontiers in microbiology · 2024Article
- Mycobacterial Regulatory Systems Involved in the Regulation of Gene Expression Under Respiration-Inhibitory Conditions.Journal of microbiology (Seoul, Korea) · 2023Review
- DosR's multifaceted role onFrontiers in cellular and infection microbiology · 2023Article
- Negative regulation of the acsA1 gene encoding the major acetyl-CoA synthetase by cAMP receptor protein in Mycobacterium smegmatis.Journal of microbiology (Seoul, Korea) · 2022Article
- Activation of the SigE-SigB signaling pathway by inhibition of the respiratory electron transport chain and its effect on rifampicin resistance in Mycobacterium smegmatis.Journal of microbiology (Seoul, Korea) · 2022Article
- Targeting Non-ReplicatingInternational journal of molecular sciences · 2021Review
- Understanding Metabolic Remodeling inFrontiers in microbiology · 2021Article
- InhibitingACS chemical biology · 2020Article
- The Partner Switching System of the SigF Sigma Factor inFrontiers in microbiology · 2020Article
- Induction of theFrontiers in microbiology · 2020Article
- Dual control of RegX3 transcriptional activity by SenX3 and PknB.The Journal of biological chemistry · 2019Article
- Inorganic polyphosphate accumulation suppresses the dormancy response and virulence inThe Journal of biological chemistry · 2019Article
- Roles of Alanine Dehydrogenase and Induction of Its Gene in Mycobacterium smegmatis under Respiration-Inhibitory Conditions.Journal of bacteriology · 2018Article
- Inhibition of the DevSR Two-Component System by Overexpression of Mycobacterium tuberculosis PknB in Mycobacterium smegmatis.Molecules and cells · 2017Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The DosS (DevS) and DosT histidine kinases form a two-component system together with the DosR (DevR) response regulator in Mycobacterium tuberculosis. DosS and DosT, which have high sequence similarity to each other over the length of their amino acid sequences, contain two GAF domains (GAF-A and GAF-B) in their N-terminal sensory domains. Complementation tests in conjunction with phylogenetic analysis showed that DevS of Mycobacterium smegmatis is more closely related to DosT than DosS. We also demonstrated in vivo that DosS and DosT of M. tuberculosis play a differential role in hypoxic adaptation. DosT responds to a decrease in oxygen tension more sensitively and strongly than DosS, which might be attributable to their different autooxidation rates. The different responsiveness of DosS and DosT to hypoxia is due to the difference in their GAF-A domains accommodating the hemes. Multiple alignment analysis of the GAF-A domains of mycobacterial DosS (DosT) homologs and subsequent site-directed mutagenesis revealed that just one substitution of E87, D90, H97, L118, or T169 of DosS with the corresponding residue of DosT is sufficient to convert DosS to DosT with regard to the responsiveness to changes in oxygen tension.
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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.