2003
Mg2+ Sensing by the Mg2+ Sensor PhoQ of Salmonella enterica
Chamnongpol S, Cromie M, Groisman EA. Mg2+ Sensing by the Mg2+ Sensor PhoQ of Salmonella enterica. Journal Of Molecular Biology 2003, 325: 795-807. PMID: 12507481, DOI: 10.1016/s0022-2836(02)01268-8.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmino Acid SubstitutionBacterial ProteinsBase SequenceBinding SitesConserved SequenceDNA, BacterialMagnesiumMolecular Sequence DataMutagenesis, Site-DirectedPhosphorylationProtein Structure, TertiaryRecombinant ProteinsSalmonella entericaSequence Homology, Amino AcidTranscription, GeneticConceptsTranscription of PhoPPhoQ proteinSensor PhoQPeriplasmic domainTwo-component regulatory systemResponse regulator PhoPExpression of phoPPhoP/PhoQWild-type responseWild-type abilityAmino acid residuesGram-negative speciesRegulator PhoPGene transcriptionPhoPAcid residuesTranscriptionHistidine residuesPhoQGenesAcetyl phosphateRegulatory systemProteinMutantsSalmonella enterica
2000
A small protein that mediates the activation of a two‐component system by another two‐component system
Kox L, Wösten M, Groisman E. A small protein that mediates the activation of a two‐component system by another two‐component system. The EMBO Journal 2000, 19: 1861-1872. PMID: 10775270, PMCID: PMC302009, DOI: 10.1093/emboj/19.8.1861.Peer-Reviewed Original ResearchMeSH KeywordsAnti-Bacterial AgentsBacterial ProteinsBase SequenceDrug Resistance, MicrobialIronMagnesiumModels, BiologicalMolecular Sequence DataMutagenesisMutationPhosphorylationPlasmidsPolymyxinsProtein BindingRecombinant ProteinsRNA Processing, Post-TranscriptionalSalmonella entericaSignal TransductionSingle-Strand Specific DNA and RNA EndonucleasesTranscription FactorsTranscription, GeneticConceptsTwo-component systemTranscription of PmrAPost-transcriptional levelExpression of pmrAPeptide antibiotic polymyxin BPmrD proteinPhoP-PhoQTranscriptional activationGenetic basisHeterologous promoterPmrA-PmrBSmall proteinsGenesPhoP-PhoQ.PmrB proteinAntimicrobial proteinsPhoQ genesProteinPmrAPhoPTranscriptionSalmonella entericaAntibiotic polymyxin BPmrDHigh iron
1997
Characterization of the Bacterial Sensor Protein PhoQ EVIDENCE FOR DISTINCT BINDING SITES FOR Mg2+ AND Ca2+ *
Véscovi E, Ayala Y, Di Cera E, Groisman E. Characterization of the Bacterial Sensor Protein PhoQ EVIDENCE FOR DISTINCT BINDING SITES FOR Mg2+ AND Ca2+ *. Journal Of Biological Chemistry 1997, 272: 1440-1443. PMID: 8999810, DOI: 10.1074/jbc.272.3.1440.Peer-Reviewed Original ResearchConceptsTranscription of PhoPPhoQ proteinDistinct binding sitesTwo-component regulatory systemGram-negative bacterium Salmonella typhimuriumPhoP/PhoQSingle amino acid substitutionBacterium Salmonella typhimuriumTryptophan intrinsic fluorescenceBinding sitesAmino acid substitutionsPeriplasmic domainAcid polypeptide
1994
A Salmonella protein that is required for resistance to antimicrobial peptides and transport of potassium.
Parra‐Lopez C, Lin R, Aspedon A, Groisman EA. A Salmonella protein that is required for resistance to antimicrobial peptides and transport of potassium. The EMBO Journal 1994, 13: 3964-3972. PMID: 8076592, PMCID: PMC395316, DOI: 10.1002/j.1460-2075.1994.tb06712.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceBiological TransportCarrier ProteinsCloning, MolecularDrug Resistance, MicrobialMelittenMembrane ProteinsMolecular Sequence DataNADPeptidesPotassiumProtaminesReceptor, trkARecombinant ProteinsRestriction MappingSalmonella typhimuriumSequence Analysis, DNASequence Homology, Amino AcidConceptsE. coli proteinsAntimicrobial peptidesMolecular genetic analysisAntimicrobial peptide protaminePutative transportersTransport of peptidesColi proteinsSingle mutantsSalmonella proteinsSame resistance pathwaysSAP mutantsHost defense moleculesGenetic analysisDefense moleculesLoci participateChannel proteinsExhibit hypersensitivityEfflux proteinsUptake systemResistance pathwaysMutantsEscherichia coliProteinTransport of potassiumHost tissues