2021
Low 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
The expanded specificity and physiological role of a widespread N-degron recognin
Gao X, Yeom J, Groisman EA. The expanded specificity and physiological role of a widespread N-degron recognin. Proceedings Of The National Academy Of Sciences Of The United States Of America 2019, 116: 18629-18637. PMID: 31451664, PMCID: PMC6744884, DOI: 10.1073/pnas.1821060116.Peer-Reviewed Original ResearchConceptsN-degron pathwayN-terminusLarge hydrophobic amino acidsPhysiological roleAmino acidsN-terminal methionineFourth amino acidHydrophobic amino acidsProtease ClpAPClp proteinsProtein homeostasisProteolytic systemIntact proteinProteinTerminusPathwayClpAPDegronAlarmoneStrong preferenceOrganellesBindsBacteriumHomeostasisProteaseActivator 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
2018
Reduction in adaptor amounts establishes degradation hierarchy among protease substrates
Yeom J, Gao X, Groisman EA. Reduction in adaptor amounts establishes degradation hierarchy among protease substrates. Proceedings Of The National Academy Of Sciences Of The United States Of America 2018, 115: e4483-e4492. PMID: 29686082, PMCID: PMC5948988, DOI: 10.1073/pnas.1722246115.Peer-Reviewed Original ResearchMeSH KeywordsBacterial ProteinsBase SequenceCarrier ProteinsEscherichia coliEscherichia coli ProteinsProteolysisSalmonellaSequence HomologySubstrate SpecificityConceptsRegulatory protein PhoPATP-dependent proteaseCritical cellular processesExpression of genesCellular processesAntibiotic persistersCytoplasmic MgProtease substratesUvrYDifferential stabilityProteasePhoPPhysiological conditionsGenesAdaptorAbundanceUnfoldaseFtsATranscriptionSubunitsSubstrateProteolysisVirulenceProteinBinds
2017
Sequestration from Protease Adaptor Confers Differential Stability to Protease Substrate
Yeom J, Wayne KJ, Groisman EA. Sequestration from Protease Adaptor Confers Differential Stability to Protease Substrate. Molecular Cell 2017, 66: 234-246.e5. PMID: 28431231, PMCID: PMC5424706, DOI: 10.1016/j.molcel.2017.03.009.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBacterial ProteinsBinding, CompetitiveCation Transport ProteinsEndopeptidase ClpGene Expression Regulation, BacterialHalf-LifeModels, MolecularMutationProtein BindingProtein Interaction Domains and MotifsProtein StabilityProteolysisSalmonella typhimuriumStructure-Activity RelationshipSubstrate SpecificityTime FactorsTranscription, GeneticConceptsN-terminal residuesSpecific N-terminal residuesRegulatory protein PhoPN-end ruleProtease ClpAPTemporal transcriptionMgtC geneN-terminusPhoPSpecific substratesClpAPDifferential stabilityProtein levelsGenesMgtCResiduesTranscriptionTerminusProteolysisProteinSubstrateProteaseBacteriaDegradationSequestration
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