ArticleJournal of bacteriology2004
Mutational analysis of the signal-sensing domain of ResE histidine kinase from Bacillus subtilis.
Article in Journal of bacteriology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 25 citations in OpenAlex.
- Shedding light on YfhS and YjlC: novel effectors of the NADH dehydrogenase activity of the electron transport chain inbioRxiv : the preprint server for biology · 2026Article
- Allosteric mechanism of signal transduction in the two-component system histidine kinase PhoQ.eLife · 2021Article
- ResDE Two-Component Regulatory System Mediates Oxygen Limitation-Induced Biofilm Formation by Bacillus amyloliquefaciens SQR9.Applied and environmental microbiology · 2018Article
- The Structure of the Periplasmic Sensor Domain of the Histidine Kinase CusS Shows Unusual Metal Ion Coordination at the Dimeric Interface.Biochemistry · 2016Article
- In vivo characterization of the scaffold activity of flotillin on the membrane kinase KinC of Bacillus subtilis.Microbiology (Reading, England) · 2015Article
- A nitric oxide regulated small RNA controls expression of genes involved in redox homeostasis in Bacillus subtilis.PLoS genetics · 2015Article
- The role of nitric-oxide-synthase-derived nitric oxide in multicellular traits of Bacillus subtilis 3610: biofilm formation, swarming, and dispersal.BMC microbiology · 2011Article
- Nitric oxide-sensitive and -insensitive interaction of Bacillus subtilis NsrR with a ResDE-controlled promoter.Molecular microbiology · 2010Article
- Kinetic characterization of the WalRKSpn (VicRK) two-component system of Streptococcus pneumoniae: dependence of WalKSpn (VicK) phosphatase activity on its PAS domain.Journal of bacteriology · 2010Article
- Transcription Factor NsrR from Bacillus subtilis Senses Nitric Oxide with a 4Fe-4S Cluster (†).Biochemistry · 2008Article
- The role of DNA-binding specificity in the evolution of bacterial regulatory networks.Journal of molecular biology · 2008Article
- Anaerobic gene expression in Staphylococcus aureus.Journal of bacteriology · 2007Article
- Control of enterotoxin gene expression in Bacillus cereus F4430/73 involves the redox-sensitive ResDE signal transduction system.Journal of bacteriology · 2006Article
- The nitric oxide-responsive regulator NsrR controls ResDE-dependent gene expression.Journal of bacteriology · 2006Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Bacillus subtilis ResD-ResE two-component regulatory system activates genes involved in nitrate respiration in response to oxygen limitation or nitric oxide (NO). The sensor kinase ResE activates the response regulator ResD through phosphorylation, which then binds to the regulatory region of genes involved in anaerobiosis to activate their transcription. ResE is composed of an N-terminal signal input domain and a C-terminal catalytic domain. The N-terminal domain contains two transmembrane subdomains and a large extracytoplasmic loop. It also has a cytoplasmic PAS subdomain between the HAMP linker and C-terminal kinase domain. In an attempt to identify the signal-sensing subdomain of ResE, a series of deletions and amino acid substitutions were generated in the N-terminal domain. The results indicated that cytoplasmic ResE lacking the transmembrane segments and the extracytoplasmic loop retains the ability to sense oxygen limitation and NO, which leads to transcriptional activation of ResDE-dependent genes. This activity was eliminated by the deletion of the PAS subdomain, demonstrating that the PAS subdomain participates in signal reception. The study also raised the possibility that the extracytoplasmic region may serve as a second signal-sensing subdomain. This suggests that the extracytoplasmic region could contribute to amplification of ResE activity leading to the robust activation of genes required for anaerobic metabolism in B. subtilis.
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