ArticleCell chemical biology2016
Basis of Mutual Domain Inhibition in a Bacterial Response Regulator.
Article in Cell chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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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
12 citing papers in PubMed.
- Constitutive activation of a hybrid two-component regulator reveals cross-regulation of polysaccharide utilization genes in Bacteroides.The Journal of biological chemistry · 2026Article
- Variations in kinase and effector signaling logic in a bacterial two component signaling network.The Journal of biological chemistry · 2025Article
- Variations in kinase and effector signaling logic in a bacterial two component signaling network.bioRxiv : the preprint server for biology · 2025Article
- Article
- Residue coevolution and mutational landscape for OmpR and NarL response regulator subfamilies.Biophysical journal · 2024Article
- Structure of phosphorylated-like RssB, the adaptor delivering σThe Journal of biological chemistry · 2023Article
- β-Lactams against the Fortress of the Gram-PositiveChemical reviews · 2021Review
- Modulation of Response Regulator CheY Reaction Kinetics by Two Variable Residues That Affect Conformation.Journal of bacteriology · 2020Article
- Shining light on the alphaproteobacterial general stress response: Comment on: Fiebig et al., Mol Microbiol, 2019.Molecular microbiology · 2019Article
- Structural basis for inhibition of a response regulator of σGenes & development · 2019Article
- Blue-Light Receptors for Optogenetics.Chemical reviews · 2018Review
- Allosteric control of a bacterial stress response system by an anti-σ factor.Molecular 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
2 authors.
Funding
Abstract
Information transmission in biological signaling networks is commonly considered to be a unidirectional flow of information between protein partners. According to this view, many bacterial response regulator proteins utilize input receiver (REC) domains to "switch" functional outputs, using REC phosphorylation to shift pre-existing equilibria between inactive and active conformations. However, recent data indicate that output domains themselves also shift such equilibria, implying a "mutual inhibition" model. Here we use solution nuclear magnetic resonance to provide a mechanistic basis for such control in a PhyR-type response regulator. Our structure of the isolated, non-phosphorylated REC domain surprisingly reveals a fully active conformation, letting us identify structural and dynamic changes imparted by the output domain to inactivate the full-length protein. Additional data reveal transient structural changes within the full-length protein, facilitating activation. Our data provide a basis for understanding the changes that REC and output domains undergo to set a default "inactive" state.
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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.