2022
An RNA-binding protein acts as a major post-transcriptional modulator in Bacillus anthracis
Pi H, Weiss A, Laut C, Grunenwald C, Lin H, Yi X, Stauff D, Skaar E. An RNA-binding protein acts as a major post-transcriptional modulator in Bacillus anthracis. Nature Communications 2022, 13: 1491. PMID: 35314695, PMCID: PMC8938561, DOI: 10.1038/s41467-022-29209-4.Peer-Reviewed Original ResearchMeSH KeywordsBacillus anthracisBacterial ProteinsCell WallGene Expression Regulation, BacterialHumansRNA-Binding ProteinsConceptsHuman pathogen Bacillus anthracisRNA-binding proteinPost-transcriptional modulatorsPathogen Bacillus anthracisDetectable nuclease activityTwo-component systemBacillus anthracisGenetic competenceRNA turnoverDNA repairMRNA stabilityCellular metabolismNuclease activityEnvelope damageRNAProteinMultiple processesAnthracisHITRSporulationGenesMRNAExpressionMetabolismTurnover
2021
DnaJ and ClpX Are Required for HitRS and HssRS Two-Component System Signaling in Bacillus anthracis
Laut C, Leasure C, Pi H, Carlin S, Chu M, Hillebrand G, Lin H, Yi X, Stauff D, Skaar E. DnaJ and ClpX Are Required for HitRS and HssRS Two-Component System Signaling in Bacillus anthracis. Infection And Immunity 2021, 90: e00560-21. PMID: 34748369, PMCID: PMC8788696, DOI: 10.1128/iai.00560-21.Peer-Reviewed Original ResearchConceptsTwo-component systemGene expressionSubstrate-binding subunitSignal transduction activityTarget gene expressionB. anthracisBacillus anthracisGram-positive bacteriumHost-induced stressesClpXP proteaseProtein chaperonesSignal transductionClpXGene productsTransduction activityDnaJVertebrate hostsHeme levelsHomeostasis regulatorGenetic selectionHigh heme levelsCell envelope disruptionBioterror weaponHssRSAnthracis
2020
Directed evolution reveals the mechanism of HitRS signaling transduction in Bacillus anthracis
Pi H, Chu M, Ivan S, Latario C, Toth A, Carlin S, Hillebrand G, Lin H, Reppart J, Stauff D, Skaar E. Directed evolution reveals the mechanism of HitRS signaling transduction in Bacillus anthracis. PLOS Pathogens 2020, 16: e1009148. PMID: 33362282, PMCID: PMC7790381, DOI: 10.1371/journal.ppat.1009148.Peer-Reviewed Original ResearchMeSH KeywordsBacillus anthracisBacterial ProteinsGene Expression Regulation, BacterialSelection, GeneticSignal TransductionStress, PhysiologicalConceptsHAMP domainSignal transductionGenetic selectionUnbiased genetic selectionCell envelope stressPathogen Bacillus anthracisSignal transduction systemImportant signal transduction systemMechanistic understandingBacillus anthracisComprehensive mechanistic understandingNumerous point mutationsEnvelope stressTransduction systemMolecular basisMutational analysisPoint mutationsTransductionRate-limiting stepIndividual domainsSpecific interactionsSignal sensingHITRAnthracisSystematic characterizationDysregulation of Magnesium Transport Protects Bacillus subtilis against Manganese and Cobalt Intoxication
Pi H, Wendel B, Helmann J. Dysregulation of Magnesium Transport Protects Bacillus subtilis against Manganese and Cobalt Intoxication. Journal Of Bacteriology 2020, 202: 10.1128/jb.00711-19. PMID: 31964700, PMCID: PMC7167470, DOI: 10.1128/jb.00711-19.Peer-Reviewed Original ResearchAdaptation, BiologicalBacillus subtilisBacterial ProteinsBiological TransportCobaltGene Expression Regulation, BacterialIronMagnesiumManganeseModels, BiologicalOperon
2018
Genome-Wide Characterization of the Fur Regulatory Network Reveals a Link between Catechol Degradation and Bacillibactin Metabolism in Bacillus subtilis
Pi H, Helmann J. Genome-Wide Characterization of the Fur Regulatory Network Reveals a Link between Catechol Degradation and Bacillibactin Metabolism in Bacillus subtilis. MBio 2018, 9: 10.1128/mbio.01451-18. PMID: 30377275, PMCID: PMC6212828, DOI: 10.1128/mbio.01451-18.Peer-Reviewed Original ResearchConceptsRegulatory networksCatechol degradationPutative DNA binding sitesGenome-wide identificationGenome-wide characterizationFerric uptake regulatorIron-dependent transcriptional repressorCellular iron requirementsDNA binding sitesIron-sufficient conditionsIron-limiting conditionsHigh-affinity iron chelatorsEnvironmental aromatic compoundsSiderophore bacillibactinFur regulonGenomic viewApo-FurRepressor functionTranscriptional repressorRegulated genesChromatin immunoprecipitationPositive regulatorIron acquisitionNegative regulationGenetic analysis
2017
Sequential induction of Fur-regulated genes in response to iron limitation in Bacillus subtilis
Pi H, Helmann J. Sequential induction of Fur-regulated genes in response to iron limitation in Bacillus subtilis. Proceedings Of The National Academy Of Sciences Of The United States Of America 2017, 114: 12785-12790. PMID: 29133393, PMCID: PMC5715773, DOI: 10.1073/pnas.1713008114.Peer-Reviewed Original ResearchMeSH KeywordsBacillus subtilisBacterial ProteinsBenzamidesCarrier ProteinsFerric CompoundsFlavodoxinGene Expression Regulation, BacterialHomeostasisIronListeria monocytogenesOligopeptidesOperonRegulonRepressor ProteinsSiderophoresConceptsFerric uptake regulatorHigh-affinity FeIron availabilityPerR regulonFur regulonSiderophore bacillibactinGenetic toolsChIP experimentsIron limitationCell transitionBacillus subtilisHigh-affinity bindingIron homeostasisBacterial cellsIntracellular ironSequential inductionRegulonBacillibactinEnzyme accessVivo occupancyGenesFurIron poolIron sufficiencyEfflux transporters
2016
The Listeria monocytogenes Fur‐regulated virulence protein FrvA is an Fe(II) efflux P1B4‐type ATPase
Pi H, Patel S, Argüello J, Helmann J. The Listeria monocytogenes Fur‐regulated virulence protein FrvA is an Fe(II) efflux P1B4‐type ATPase. Molecular Microbiology 2016, 100: 1066-1079. PMID: 26946370, PMCID: PMC4914386, DOI: 10.1111/mmi.13368.Peer-Reviewed Original Research
2012
A Putative P-Type ATPase Required for Virulence and Resistance to Haem Toxicity in Listeria monocytogenes
McLaughlin H, Xiao Q, Rea R, Pi H, Casey P, Darby T, Charbit A, Sleator R, Joyce S, Cowart R, Hill C, Klebba P, Gahan C. A Putative P-Type ATPase Required for Virulence and Resistance to Haem Toxicity in Listeria monocytogenes. PLOS ONE 2012, 7: e30928. PMID: 22363518, PMCID: PMC3283593, DOI: 10.1371/journal.pone.0030928.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesAnimalsBacterial ProteinsBase SequenceBiological AssayComputational BiologyDrug Resistance, BacterialGene Expression Regulation, BacterialGenes, BacterialGenetic LociHemeHomeostasisIronListeria monocytogenesListeriosisMiceMolecular Sequence DataMothsMutagenesis, InsertionalMutationPlasmidsReal-Time Polymerase Chain ReactionRepressor ProteinsVirulenceConceptsPutative P-type ATPaseFerric uptake regulatorUptake of haemIntracellular pathogen Listeria monocytogenesWax moth Galleria mellonellaP-type ATPaseAcquisition of ironPathogen Listeria monocytogenesMoth Galleria mellonellaIron-deficient mediumMembrane proteinsMutantsHaem toxicityFree haemAlternative infection modelGalleria mellonellaIron homeostasisInhibition of growthFrvAVirulenceListeria monocytogenesHaemVirulence potentialFurDeficient medium