2010
Quantitative Characterization of the Interactions among c-myc Transcriptional Regulators FUSE, FBP, and FIR
Hsiao HH, Nath A, Lin CY, Folta-Stogniew EJ, Rhoades E, Braddock DT. Quantitative Characterization of the Interactions among c-myc Transcriptional Regulators FUSE, FBP, and FIR. Biochemistry 2010, 49: 4620-4634. PMID: 20420426, DOI: 10.1021/bi9021445.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceCarrier ProteinsDimerizationDNA HelicasesDNA-Binding ProteinsGuanine Nucleotide Exchange FactorsHumansModels, MolecularMolecular Sequence DataNucleic Acid ConformationProtein BindingProto-Oncogene Proteins c-mycRepressor ProteinsRho Guanine Nucleotide Exchange FactorsRNA Splicing FactorsRNA-Binding ProteinsSolutionsTrans-ActivatorsConceptsDNA strand preferencesProtein-DNA interactionsC-myc transcriptionPotent oncogenic factorHuman c-mycFBP bindsTranscriptional regulationActive transcriptionNear-physiological conditionsTripartite interactionCell homeostasisInhibitory complexStrand preferenceC-MycOncogenic factorRegulatory systemUnique modeTranscriptionStrand DNABiological experimentsComplex formationLow micromolar rangeDNADifferent conformationsMicromolar range
2009
Structural Characterization of the E2 Domain of APL-1, a Caenorhabditis elegans Homolog of Human Amyloid Precursor Protein, and Its Heparin Binding Site*
Hoopes JT, Liu X, Xu X, Demeler B, Folta-Stogniew E, Li C, Ha Y. Structural Characterization of the E2 Domain of APL-1, a Caenorhabditis elegans Homolog of Human Amyloid Precursor Protein, and Its Heparin Binding Site*. Journal Of Biological Chemistry 2009, 285: 2165-2173. PMID: 19906646, PMCID: PMC2804372, DOI: 10.1074/jbc.m109.018432.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmyloid beta-Protein PrecursorAnimalsBinding SitesCaenorhabditis elegansCaenorhabditis elegans ProteinsCrystallography, X-RayHeparinHumansHydrogen-Ion ConcentrationMembrane ProteinsModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedMutationProtein StabilityProtein Structure, TertiarySequence Homology, Amino AcidSolutionsSucrose
2008
Reexamination of the Role of the Amino Terminus of SecA in Promoting Its Dimerization and Functional State
Das S, Stivison E, Folta-Stogniew E, Oliver D. Reexamination of the Role of the Amino Terminus of SecA in Promoting Its Dimerization and Functional State. Journal Of Bacteriology 2008, 190: 7302-7307. PMID: 18723626, PMCID: PMC2580686, DOI: 10.1128/jb.00593-08.Peer-Reviewed Original ResearchConceptsWild-type SecAProtein-conducting channelCell growthAmino-terminal regionSecA dimerSecA functionsProtein translocationSecA expressionMembrane associationMutant proteinsCell fractionationATPase specific activityCorresponding proteinProtein cargoCarboxyl terminusAmino terminusVivo functionSecADimerization defectFunctional stateMutantsBiochemical studiesResidue resultsProteinChemical cross
2007
Dimerization of FIR upon FUSE DNA binding suggests a mechanism of c‐myc inhibition
Crichlow GV, Zhou H, Hsiao HH, Frederick KB, Debrosse M, Yang Y, Folta-Stogniew EJ, Chung HJ, Fan C, De La Cruz EM, Levens D, Lolis E, Braddock D. Dimerization of FIR upon FUSE DNA binding suggests a mechanism of c‐myc inhibition. The EMBO Journal 2007, 27: 277-289. PMID: 18059478, PMCID: PMC2206118, DOI: 10.1038/sj.emboj.7601936.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCrystallography, X-RayDimerizationDNADNA HelicasesDNA-Binding ProteinsDrosophila ProteinsGene Expression RegulationHumansMagnetic Resonance SpectroscopyMolecular Sequence DataPromoter Regions, GeneticProtein BindingProto-Oncogene Proteins c-mycRepressor ProteinsRNA Splicing FactorsRNA-Binding ProteinsTranscription Factor TFIIHConceptsRRM domainDNA bindingFirst RRM domainSecond RRM domainC-myc transcriptional controlSite-directed mutationsDNA upstreamTranscriptional controlInfluences transcriptionC-Myc inhibitionNucleic acid recognitionPromoter sitesP1 promoterAnalogous mutationCell homeostasisC-MycTFIIHProteinLight scattering revealBinding sitesDNATranscriptionSingle strandsMutationsSize exclusion chromatographyThe structural basis of cyclic diguanylate signal transduction by PilZ domains
Benach J, Swaminathan SS, Tamayo R, Handelman SK, Folta‐Stogniew E, Ramos JE, Forouhar F, Neely H, Seetharaman J, Camilli A, Hunt JF. The structural basis of cyclic diguanylate signal transduction by PilZ domains. The EMBO Journal 2007, 26: 5153-5166. PMID: 18034161, PMCID: PMC2140105, DOI: 10.1038/sj.emboj.7601918.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBacterial ProteinsBinding SitesCrystallography, X-RayCyclic GMPHumansMiceModels, MolecularMolecular ConformationMolecular Sequence DataPhylogenyProtein BindingProtein Structure, QuaternaryProtein Structure, SecondaryProtein Structure, TertiarySequence AlignmentSequence Homology, Amino AcidSignal TransductionVibrio choleraeConceptsPilZ domain-containing proteinsPilZ domainDomain-containing proteinsN-terminal domainConformational switchSecond messenger cyclic diguanylateBeta-barrel foldN-terminal loopEvolutionary diversificationCyclic diguanylateSignal transductionBioinformatics analysisStructural basisInteraction surfaceSessile growthEffector pathwaysVibrio choleraeProteinV. choleraeGMPCholeraeDomainClose appositionDiguanylateEubacteria
2003
Trimeric Subunit Stoichiometry of the Glutamate Transporters from Bacillus caldotenax and Bacillus stearothermophilus †
Yernool D, Boudker O, Folta-Stogniew E, Gouaux E. Trimeric Subunit Stoichiometry of the Glutamate Transporters from Bacillus caldotenax and Bacillus stearothermophilus †. Biochemistry 2003, 42: 12981-12988. PMID: 14596613, DOI: 10.1021/bi030161q.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmino Acid Transport System X-AGBacillusChromatography, GelCross-Linking ReagentsElectrophoresis, Polyacrylamide GelGenetic VectorsGeobacillus stearothermophilusGlutaralLasersLiposomesMolecular Sequence DataMolecular WeightProtein SubunitsProtein TransportScattering, RadiationSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationSpectrophotometry, UltravioletConceptsSubunit stoichiometryBacillus caldotenaxMembrane proteinsPolytopic integral membrane proteinPrimary structureAmino acid sequence relationshipsGlutamate transportersBacillus stearothermophilusKingdoms of lifeIntegral membrane proteinsNeutral amino acid transporterTrimeric quaternary structureNative molecular massDetergent-solubilized stateAmino acid transportersSize exclusion chromatographyB. caldotenaxEukaryotic organismsHigh-affinity glutamate transportersEukaryotic transportersQuaternary organizationAqueous solutionNutrient uptakeLife formsDetergent micelles