2021
RNA chaperone activates Salmonella virulence program during infection
Choi J, Salvail H, Groisman EA. RNA chaperone activates Salmonella virulence program during infection. Nucleic Acids Research 2021, 49: 11614-11628. PMID: 34751407, PMCID: PMC8599858, DOI: 10.1093/nar/gkab992.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBacterial ProteinsCell LineHeat-Shock ProteinsMacrophagesMembrane ProteinsMiceRNA StabilityRNA, MessengerSalmonella typhimuriumConceptsPhoP activationVirulence regulator PhoPWild-type virulenceBacterium Salmonella enterica serovar TyphimuriumWild-type S. typhimuriumSalmonella enterica serovar TyphimuriumRNA chaperonesEnterica serovar TyphimuriumRegulator PhoPRedundant proteinsMutant behavesVirulence programVirulence roleS. typhimuriumInside macrophagesSecondary structureSerovar TyphimuriumCritical functionsVirulence genesChaperonesPhoPMutantsRibosomesOrganismsCSPCLow Cytoplasmic Magnesium Increases the Specificity of the Lon and ClpAP Proteases
Yeom J, Groisman EA. Low Cytoplasmic Magnesium Increases the Specificity of the Lon and ClpAP Proteases. Journal Of Bacteriology 2021, 203: 10.1128/jb.00143-21. PMID: 33941609, PMCID: PMC8223949, DOI: 10.1128/jb.00143-21.Peer-Reviewed Original ResearchMeSH KeywordsBacterial ProteinsCytoplasmGene Expression Regulation, BacterialHeat-Shock ProteinsMagnesiumProtease LaSalmonella typhimuriumSubstrate SpecificityConceptsBacterium Salmonella enterica serovar TyphimuriumCytoplasmic MgSalmonella enterica serovar TyphimuriumLon substratesClpAP proteaseEnterica serovar TyphimuriumAntibiotic persistenceEnteric bacteriaSerovar TyphimuriumSpectrum of substratesPhoP proteinProtease LonAcetyl coenzyme ATranscriptional regulatorsProtein bindsPhoP boxRegulatory proteinsProtease specificityPromoter regionCritical regulatorProtein synthesisLiving cellsLonPhoPEscherichia coli
2019
Activator of one protease transforms into inhibitor of another in response to nutritional signals
Yeom J, Groisman EA. Activator of one protease transforms into inhibitor of another in response to nutritional signals. Genes & Development 2019, 33: 1280-1292. PMID: 31371438, PMCID: PMC6719616, DOI: 10.1101/gad.325241.119.Peer-Reviewed Original ResearchConceptsNutritional signalsProtease specificityClpAP proteaseProtease LonProtein homeostasisParticular proteinToxic proteinsRegulatory roleParticular substrateRapid response mechanismProtein amountSpecific signalsResponse mechanismsProteaseProteinActivatorAcetylationProteomeCellsInhibitorsLonAdaptorSpecificityProteolysisBinds