2022
Gut Commensal Bacteroidetes Encode a Novel Class of Vitamin B12-Binding Proteins
Putnam EE, Abellon-Ruiz J, Killinger BJ, Rosnow JJ, Wexler AG, Folta-Stogniew E, Wright AT, van den Berg B, Goodman AL. Gut Commensal Bacteroidetes Encode a Novel Class of Vitamin B12-Binding Proteins. MBio 2022, 13: e02845-21. PMID: 35227073, PMCID: PMC8941943, DOI: 10.1128/mbio.02845-21.Peer-Reviewed Original ResearchConceptsComplex microbial communitiesHuman gut commensalTerminal globular domainModel organismsGut microbiomeMicrobial communitiesCompetitive fitnessTransport systemStructural homologsAccessory proteinsNew proteinsAdditional proteinsTransport proteinsGlobular domainUnknown functionMultiple transport systemsSystem lociKey roleGut commensalsProteinDiverse repertoireRelated moleculesMajor groupsFitnessOrganisms
2013
Oligomerization and higher‐order assembly contribute to sub‐cellular localization of a bacterial scaffold
Bowman GR, Perez AM, Ptacin JL, Ighodaro E, Folta‐Stogniew E, Comolli LR, Shapiro L. Oligomerization and higher‐order assembly contribute to sub‐cellular localization of a bacterial scaffold. Molecular Microbiology 2013, 90: 776-795. PMID: 24102805, PMCID: PMC3859194, DOI: 10.1111/mmi.12398.Peer-Reviewed Original ResearchConceptsSub-cellular localizationAmino acidsN-terminal 23 amino acidsDefective mutant proteinsAsymmetric cell divisionC-terminal 76 amino acidsC-terminal domainDimer of trimersCaulobacter crescentusCell polesLocalization determinantsHigher-order structureMutant proteinsScaffold proteinSubcellular fociCell divisionLinker domainPopZMutational analysisBiophysical analysisWild typePolar organizationOrganizing centerDistinct setsProtein
2009
Macromolecular Interactions: Light Scattering
Folta‐Stogniew E. Macromolecular Interactions: Light Scattering. 2009 DOI: 10.1002/9780470015902.a0003143.Peer-Reviewed Original ResearchMolar massTranslational diffusion coefficientRadius of gyrationSpectroscopic techniquesAssociation stoichiometryDynamic lightBiological macromoleculesHydrodynamic radiusLight scatteringOligomeric stateStatic lightStructural studiesModified proteinsNucleic acidsSLS experimentsPhospholipid vesiclesDiffusion coefficientMacromoleculesProtein stockProteinMonodispersityDLSNanoparticlesHomoDetermination
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
2004
Exchange of DNA Base Pairs that Coincides with Recognition of Homology Promoted by E. coli RecA Protein
Folta-Stogniew E, O'Malley S, Gupta R, Anderson KS, Radding CM. Exchange of DNA Base Pairs that Coincides with Recognition of Homology Promoted by E. coli RecA Protein. Molecular Cell 2004, 15: 965-975. PMID: 15383285, DOI: 10.1016/j.molcel.2004.08.017.Peer-Reviewed Original ResearchConceptsE. coli RecA proteinRecognition of homologyColi RecA proteinRecA proteinBase pairsStrand exchangeSynaptic complexDouble-strand breaksT base pairsStopped-flow fluorescenceGenetic recombinationSingle strandsHomologyUnresolved mechanismDuplex DNADNA base pairsDNARate of exchangeProteinDynamic structureComplexesStrandsBasis exchangeRate of formationMechanism
1999
Rapid Exchange of A:T Base Pairs Is Essential for Recognition of DNA Homology by Human Rad51 Recombination Protein
Gupta R, Folta-Stogniew E, O'Malley S, Takahashi M, Radding C. Rapid Exchange of A:T Base Pairs Is Essential for Recognition of DNA Homology by Human Rad51 Recombination Protein. Molecular Cell 1999, 4: 705-714. PMID: 10619018, DOI: 10.1016/s1097-2765(00)80381-0.Peer-Reviewed Original ResearchConceptsRecognition of homologyBase pairsRad51 recombination proteinT base pairsRecombination proteinsHuman Rad51Genetic exchangeFluorescence resonance energy transferUbiquitous familyMechanism of recognitionDNA repairStrand exchangeDNA homologyBase substitutionsHomologyResonance energy transferDuplex DNAHelix destabilizationCritical roleBase mismatchesProteinSingle strandsRAD51Rapid exchangeKinetic analysisDetermination of molecular masses of proteins in solution: Implementation of an HPLC size exclusion chromatography and laser light scattering service in a core laboratory.
Folta-Stogniew E, Williams KR. Determination of molecular masses of proteins in solution: Implementation of an HPLC size exclusion chromatography and laser light scattering service in a core laboratory. Journal Of Biomolecular Techniques 1999, 10: 51-63. PMID: 19499008, PMCID: PMC2291588.Peer-Reviewed Original ResearchRefractive indexLaser lightSEC/LSEmission spectraAbsorption spectraLight scatteringSize exclusion chromatographyInstrument configurationLS experimentsProtein oligomerizationNative proteinRI detectorMolecular massNonglobular shapeSpectraMolecular weightProteinHPLC size exclusion chromatographyMW determinationLaserLightScatteringExclusion chromatographyProtein standardsDetectorHuman Rad51 Protein Can Form Homologous Joints in the Absence of Net Strand Exchange*
Gupta R, Folta-Stogniew E, Radding C. Human Rad51 Protein Can Form Homologous Joints in the Absence of Net Strand Exchange*. Journal Of Biological Chemistry 1999, 274: 1248-1256. PMID: 9880493, DOI: 10.1074/jbc.274.3.1248.Peer-Reviewed Original ResearchConceptsStrand exchangeRecA proteinEscherichia coli RecA proteinColi RecA proteinHuman Rad51 proteinDNA strand exchange reactionStrand exchange reactionEukaryotic homologsHsRad51 proteinRad51 proteinHomologous pairingGC contentCentral enzymeHeteroduplex DNABiological roleHsRad51Oligonucleotide substratesRich DNAGC compositionHuman DNAProteinLinear duplexHomologous jointsDNAGC pairs
1997
RecA tests homology at both pairing and strand exchange
Bazemore L, Folta-Stogniew E, Takahashi M, Radding C. RecA tests homology at both pairing and strand exchange. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 11863-11868. PMID: 9342328, PMCID: PMC23638, DOI: 10.1073/pnas.94.22.11863.Peer-Reviewed Original Research