ArticleJournal of bacteriology2014
The PhoU protein from Escherichia coli interacts with PhoR, PstB, and metals to form a phosphate-signaling complex at the membrane.
Article in Journal of bacteriology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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Who cites it
59 citing papers in PubMed, 120 citations in OpenAlex.
- The removal of iron and phosphate from culture medium by Rhodococcus ruber SiAl.Folia microbiologica · 2026Article
- Article
- Molecular mechanism of phosphate import by the bacterial PstSCAB transporter.Nature communications · 2026Article
- Genomic insights into novelBurkholderia sp. Bmkn7 from coastal saline-affected rice fields unveils potential antimicrobial metabolites and plant growth-promoting traits.Scientific reports · 2026Article
- Microbial phenazines: biosynthesis, structural diversity, evolution, regulation, and biological significance.Microbiology and molecular biology reviews : MMBR · 2025Review
- Roles of Pho regulon in bacterial pathogenicity.Virulence · 2025Review
- Multiple clades of regulators contribute to bacterial phosphate homeostasis and pathogenesis.bioRxiv : the preprint server for biology · 2025Article
- PhoU interaction with the PhoR PAS domain is required for repression of the pho regulon and Salmonella virulence, but not for polyphosphate accumulation.Journal of microbiology (Seoul, Korea) · 2025Article
- Biodegradation of glyphosate by Stenotrophomonas maltophilia GP-1 involves C-P lyase pathway.Biodegradation · 2025Article
- Loss of LasR function leads to decreased repression ofJournal of bacteriology · 2025Article
- The adjacent ATP-binding protein-encoding genes of theJournal of bacteriology · 2025Article
- Context-dependent change in the fitness effect of (in)organic phosphate antiporter glpT during Salmonella Typhimurium infection.Nature communications · 2025Article
- Small DUF1127 proteins regulate bacterial phosphate metabolism through protein-protein interactions with the sensor kinase PhoR.microLife · 2025Article
- Main controls onFrontiers in microbiology · 2025Article
- Unveiling the role of the PhoP master regulator in arsenite resistance throughCurrent research in microbial sciences · 2025Article
- An intracellular phosphorus-starvation signal activates the PhoB/PhoR two-component system inmBio · 2024Article
- Wastewater Treatment with Bacterial Representatives of theInternational journal of molecular sciences · 2024Review
- Phosphate Uptake and Its Relation to Arsenic Toxicity in Lactobacilli.International journal of molecular sciences · 2024Article
- Chemical Reaction Models in Synthetic Promoter Design in Bacteria.Methods in molecular biology (Clifton, N.J.) · 2024Article
- A Survey of Two-Component Systems in Coxiella burnetii Reveals Redundant Regulatory Schemes and a Requirement for an Atypical PhoBR System in Mammalian Cell Infection.Journal of bacteriology · 2023Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Robust growth in many bacteria is dependent upon proper regulation of the adaptive response to phosphate (Pi) limitation. This response enables cells to acquire Pi with high affinity and utilize alternate phosphorous sources. The molecular mechanisms of Pi signal transduction are not completely understood. PhoU, along with the high-affinity, Pi-specific ATP-binding cassette transporter PstSCAB and the two-component proteins PhoR and PhoB, is absolutely required for Pi signaling in Escherichia coli. Little is known about the role of PhoU and its function in regulation. We have demonstrated using bacterial two-hybrid analysis and confirmatory coelution experiments that PhoU interacts with PhoR through its PAS (Per-ARNT-Sim) domain and that it also interacts with PstB, the cytoplasmic component of the transporter. We have also shown that the soluble form of PhoU is a dimer that binds manganese and magnesium. Alteration of highly conserved residues in PhoU by site-directed mutagenesis shows that these sites play a role in binding metals. Analysis of these phoU mutants suggests that metal binding may be important for PhoU membrane interactions. Taken together, these results support the hypothesis that PhoU is involved in the formation of a signaling complex at the cytoplasmic membrane that responds to environmental Pi levels.
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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.