2013
Signal‐specific temporal response by the Salmonella PhoP/PhoQ regulatory system
Park S, Groisman EA. Signal‐specific temporal response by the Salmonella PhoP/PhoQ regulatory system. Molecular Microbiology 2013, 91: 135-144. PMID: 24256574, PMCID: PMC3890429, DOI: 10.1111/mmi.12449.Peer-Reviewed Original ResearchConceptsTransporter MgtATwo-component systems PhoP/PhoQPhoP-dependent genesAntimicrobial peptide C18G.PhoP/PhoQSalmonella enterica serovar TyphimuriumSensor PhoQEnterica serovar TyphimuriumVirulence functionsRepressing signalsGene setsPhoQMgtAGenesSerovar TyphimuriumElicit expressionPeriplasmPhoPActive formFull transcriptionExpressionPhoQ.TranscriptionCytoplasmicProtein
2006
Identification of the lipopolysaccharide modifications controlled by the Salmonella PmrA/PmrB system mediating resistance to Fe(III) and Al(III)
Nishino K, Hsu FF, Turk J, Cromie MJ, Wösten MM, Groisman EA. Identification of the lipopolysaccharide modifications controlled by the Salmonella PmrA/PmrB system mediating resistance to Fe(III) and Al(III). Molecular Microbiology 2006, 61: 645-654. PMID: 16803591, PMCID: PMC1618816, DOI: 10.1111/j.1365-2958.2006.05273.x.Peer-Reviewed Original ResearchMeSH KeywordsAluminumBacterial ProteinsBase SequenceDrug Resistance, BacterialEscherichia coli ProteinsGene Expression Regulation, BacterialIronLipid ALipopolysaccharidesMolecular Sequence DataMutationPeriplasmPhosphoric Monoester HydrolasesPhosphorylationPolymyxin BSalmonella typhimuriumSoil MicrobiologyTranscription FactorsConceptsPmrA/PmrB systemGram-negative bacterial speciesNon-host environmentsPmrA/PmrBWild-type strainSalmonella enterica serovar TyphimuriumEnterica serovar TyphimuriumOuter membraneLipopolysaccharide modificationBacterial speciesCovalent modificationResistance genesSerovar TyphimuriumOxygen-dependent killingPmrAEssential metalsHomeostatic mechanismsSalmonella survivalMutantsDephosphorylationGenesSpeciesProteinMajor constituentsIdentification
1999
A Periplasmicd-Alanyl-d-Alanine Dipeptidase in the Gram-Negative Bacterium Salmonella enterica
Hilbert F, del Portillo F, Groisman E. A Periplasmicd-Alanyl-d-Alanine Dipeptidase in the Gram-Negative Bacterium Salmonella enterica. Journal Of Bacteriology 1999, 181: 2158-2165. PMID: 10094694, PMCID: PMC93629, DOI: 10.1128/jb.181.7.2158-2165.1999.Peer-Reviewed Original ResearchConceptsD-alanyl-D-alanine dipeptidaseD-Ala-D-Ala dipeptidaseHorizontal gene transferRelated bacterial speciesSpecies Salmonella entericaEscherichia coli KSimilar substrate specificityBacterium Salmonella entericaSalmonella entericaDipeptidase geneWild-type SalmonellaPeptidoglycan metabolismSole carbon sourcePeriplasmic spaceSalmonella chromosomeSubstrate specificityD-AlaColi KBacterial speciesSalmonella enzymeVanX proteinGene transferEnzymatic activityGlycopeptide antibiotic vancomycinCarbon source