ArticleJournal of bacteriology2008
O2- and NO-sensing mechanism through the DevSR two-component system in Mycobacterium smegmatis.
Article in Journal of bacteriology, 2008. 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, 53 citations in OpenAlex.
- Immunoblot-based activity assay for heme-containing histidine kinases.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026Article
- Thermal shift assay to identify ligands for bacterial sensor proteins.FEMS microbiology reviews · 2025Review
- Mycobacterial Regulatory Systems Involved in the Regulation of Gene Expression Under Respiration-Inhibitory Conditions.Journal of microbiology (Seoul, Korea) · 2023Review
- Multistep Signaling in Nature: A Close-Up ofInternational journal of molecular sciences · 2021Review
- How Bacterial Redox Sensors Transmit Redox Signals via Structural Changes.Antioxidants (Basel, Switzerland) · 2021Review
- InhibitingACS chemical biology · 2020Article
- Induction of theFrontiers in microbiology · 2020Article
- MnoSR Is a Bona Fide Two-Component System Involved in Methylotrophic Metabolism in Mycobacterium smegmatis.Applied and environmental microbiology · 2019Article
- Inhibition of the DevSR Two-Component System by Overexpression of Mycobacterium tuberculosis PknB in Mycobacterium smegmatis.Molecules and cells · 2017Article
- Effects of nutritional and ambient oxygen condition on biofilm formation in Mycobacterium avium subsp. hominissuis via altered glycolipid expression.Scientific reports · 2017Article
- Nitrogen oxide cycle regulates nitric oxide levels and bacterial cell signaling.Scientific reports · 2016Article
- Insights into redox sensing metalloproteins in Mycobacterium tuberculosis.Journal of inorganic biochemistry · 2014Review
- Heme sensor proteins.The Journal of biological chemistry · 2013Review
- Activation of ATP binding for the autophosphorylation of DosS, a Mycobacterium tuberculosis histidine kinase lacking an ATP lid motif.The Journal of biological chemistry · 2013Article
- S-nitrosylation of phosphotransfer proteins represses cytokinin signaling.Nature communications · 2013Article
- The DosS-DosT/DosR Mycobacterial Sensor System.Biosensors · 2013Article
- WithdrawnInfectious disorders drug targets · 2012Article
- Protein-protein interactions between histidine kinases and response regulators of Mycobacterium tuberculosis H37Rv.Journal of microbiology (Seoul, Korea) · 2012Article
- Adaptation to environmental stimuli within the host: two-component signal transduction systems of Mycobacterium tuberculosis.Microbiology and molecular biology reviews : MMBR · 2011Review
- Comparative genomics of the dormancy regulons in mycobacteria.Journal of bacteriology · 2011Article
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The DevS histidine kinase of Mycobacterium smegmatis contains tandem GAF domains (GAF-A and GAF-B) in its N-terminal sensory domain. The heme iron of DevS is in the ferrous state when purified and is resistant to autooxidation from a ferrous to a ferric state in the presence of O(2). The redox property of the heme and the results of sequence comparison analysis indicate that DevS of M. smegmatis is more closely related to DosT of Mycobacterium tuberculosis than DevS of M. tuberculosis. The binding of O(2) to the deoxyferrous heme led to a decrease in the autokinase activity of DevS, whereas NO binding did not. The regulation of DevS autokinase activity in response to O(2) and NO was not observed in the DevS derivatives lacking its heme, indicating that the ligand-binding state of the heme plays an important role in the regulation of DevS kinase activity. The redox state of the quinone/quinol pool of the respiratory electron transport chain appears not to be implicated in the regulation of DevS activity. Neither cyclic GMP (cGMP) nor cAMP affected DevS autokinase activity, excluding the possibility that the cyclic nucleotides serve as the effector molecules to modulate DevS kinase activity. The three-dimensional structure of the putative GAF-B domain revealed that it has a GAF folding structure without cyclic nucleotide binding capacity.
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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.