2010
Nucleobindin 1 Is a Calcium-regulated Guanine Nucleotide Dissociation Inhibitor of Gαi1 *
Kapoor N, Gupta R, Menon ST, Folta-Stogniew E, Raleigh DP, Sakmar TP. Nucleobindin 1 Is a Calcium-regulated Guanine Nucleotide Dissociation Inhibitor of Gαi1 *. Journal Of Biological Chemistry 2010, 285: 31647-31660. PMID: 20679342, PMCID: PMC2951237, DOI: 10.1074/jbc.m110.148429.Peer-Reviewed Original ResearchConceptsNucleobindin-1Dissociation inhibitorHeterotrimeric G protein α subunitsGuanine Nucleotide Dissociation InhibitorG protein α subunitsNucleotide Dissociation InhibitorHeterotrimeric G proteinsProtein α subunitsReceptor-mediated signal transduction pathwaysSignal transduction pathwaysGoLoco motifGDI activityProtein traffickingRGS proteinsBiochemical functionsTransduction pathwaysGDP releaseΑ-subunitCalcium-binding proteinsG proteinsConformational changesBiochemical propertiesTissue culture experimentsFluorescence spectroscopy experimentsAdenylyl cyclaseQuantitative 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
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 chromatography
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 analysisHuman 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