ArticleJournal of molecular biology2009
Probing the roles of the two different dimers mediated by the receiver domain of the response regulator PhoB.
Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- Non-Canonical Inter-Protein Interactions of Key Proteins Belonging to Cytokinin Signaling Pathways.Plants (Basel, Switzerland) · 2025Review
- Acetylation of K188 and K192 inhibits the DNA-binding ability of NarL to regulateApplied and environmental microbiology · 2023Article
- Directed evolution reveals the mechanism of HitRS signaling transduction in Bacillus anthracis.PLoS pathogens · 2020Article
- New Insights into Multistep-Phosphorelay (MSP)/ Two-Component System (TCS) Regulation: Are Plants and Bacteria that Different?Plants (Basel, Switzerland) · 2019Review
- Overcoming the Cost of Positive Autoregulation by Accelerating the Response with a Coupled Negative Feedback.Cell reports · 2018Article
- Phosphate signaling through alternate conformations of the PstSCAB phosphate transporter.BMC microbiology · 2018Article
- An Adaptive Mutation in Enterococcus faecium LiaR Associated with Antimicrobial Peptide Resistance Mimics Phosphorylation and Stabilizes LiaR in an Activated State.Journal of molecular biology · 2016Article
- Experimental Analysis of Functional Variation within Protein Families: Receiver Domain Autodephosphorylation Kinetics.Journal of bacteriology · 2016Article
- Structure of the Response Regulator NsrR from Streptococcus agalactiae, Which Is Involved in Lantibiotic Resistance.PloS one · 2016Article
- Identification of the PhoB Regulon and Role of PhoU in the Phosphate Starvation Response of Caulobacter crescentus.Journal of bacteriology · 2016Article
- Imidazole as a Small Molecule Analogue in Two-Component Signal Transduction.Biochemistry · 2015Article
- The Escherichia coli NarL receiver domain regulates transcription through promoter specific functions.BMC microbiology · 2015Article
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- DNA consensus sequence motif for binding response regulator PhoP, a virulence regulator of Mycobacterium tuberculosis.Biochemistry · 2014Article
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- Article
- Atypical OmpR/PhoB subfamily response regulator GlnR of actinomycetes functions as a homodimer, stabilized by the unphosphorylated conserved Asp-focused charge interactions.The Journal of biological chemistry · 2014Article
- An asymmetric heterodomain interface stabilizes a response regulator-DNA complex.Nature communications · 2014Article
- A tale of two machines: a review of the BLAST meeting, Tucson, AZ, 20-24 January 2013.Molecular microbiology · 2014Review
- A biochemical characterization of the DNA binding activity of the response regulator VicR from Streptococcus mutans.PloS one · 2014Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Structural analysis of the Escherichia coli response regulator transcription factor PhoB indicates that the protein dimerizes in two different orientations that are both mediated by the receiver domain. The two dimers exhibit 2-fold rotational symmetry: one involves the alpha 4-beta 5-alpha 5 surface and the other involves the alpha1/alpha 5 surface. The alpha 4-beta 5-alpha 5 dimer is observed when the protein is crystallized in the presence of the phosphoryl analog BeF(3)(-), while the alpha1/alpha 5 dimer is observed in its absence. From these studies, a model of the inactive and active states of PhoB has been proposed that involves the formation of two distinct dimers. In order to gain further insight into the roles of these dimers, we have engineered a series of mutations in PhoB intended to perturb each of them selectively. Our results indicate that perturbation of the alpha 4-beta 5-alpha 5 surface disrupts phosphorylation-dependent dimerization and DNA binding as well as PhoB-mediated transcriptional activation of phoA, while perturbations to the alpha1/alpha 5 surface do not. Furthermore, experiments with a GCN4 leucine zipper/PhoB chimera protein indicate that PhoB is activated through an intermolecular mechanism. Together, these results support a model of activation of PhoB in which phosphorylation promotes dimerization via the alpha 4-beta 5-alpha 5 face, which enhances DNA binding and thus the ability of PhoB to regulate transcription.
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