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 ResearchConceptsFerric 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
2015
Origin, diversification and substrate specificity in the family of NCS1/FUR transporters
Krypotou E, Evangelidis T, Bobonis J, Pittis A, Gabaldón T, Scazzocchio C, Mikros E, Diallinas G. Origin, diversification and substrate specificity in the family of NCS1/FUR transporters. Molecular Microbiology 2015, 96: 927-950. PMID: 25712422, DOI: 10.1111/mmi.12982.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAspergillus nidulansBinding SitesFungal ProteinsGene DuplicationGene Transfer, HorizontalMembrane Transport ProteinsMolecular Docking SimulationMolecular Dynamics SimulationMutationPhylogenyProtein ConformationProtein Structure, TertiaryPseudogenesSequence Homology, Amino AcidSubstrate SpecificitySymportersConceptsSubstrate specificitySubstrate Binding SiteFunctional diversificationModel fungus Aspergillus nidulansSystematic mutational analysisBinding sitesStructure-function analysisUptake of purinesNCS1 proteinsPlant homologuesFur proteinAspergillus nidulansGene duplicationHorizontal transferSubstrate dockingMutation analysisSub-familyHomology modelingMolecular mechanismsNCS1ProteinResiduesFurDiversificationNidulans
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
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