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
2005
Hydrodynamic Characterization of the DEAD-box RNA Helicase DbpA
Talavera MA, Matthews EE, Eliason WK, Sagi I, Wang J, Henn A, De La Cruz EM. Hydrodynamic Characterization of the DEAD-box RNA Helicase DbpA. Journal Of Molecular Biology 2005, 355: 697-707. PMID: 16325852, DOI: 10.1016/j.jmb.2005.10.058.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsChromatography, GelComputersCross-Linking ReagentsDEAD-box RNA HelicasesElectrophoretic Mobility Shift AssayEscherichia coliEscherichia coli ProteinsModels, BiologicalModels, MolecularProtein Structure, TertiaryRNARNA HelicasesRNA-Binding ProteinsStructural Homology, ProteinConceptsHelicase core domainNucleic acid helicasesCarboxyl-terminal domainAb initio structure prediction methodNucleic acid unwindingHelicase activityRNA metabolismHydrodynamic bead modelingDistinct RNARNA substratesHairpin 92ATP hydrolysisStructural homologyStructure prediction methodsCore domainOligomeric formsAnalytical ultracentrifugationDbpAProtein AMulti-angle laserBead modelingRNASize exclusion chromatographyKey roleFunctional properties
2004
Equilibrium and Kinetic Analysis of Nucleotide Binding to the DEAD-Box RNA Helicase DbpA †
Talavera MA, De La Cruz EM. Equilibrium and Kinetic Analysis of Nucleotide Binding to the DEAD-Box RNA Helicase DbpA †. Biochemistry 2004, 44: 959-970. PMID: 15654752, DOI: 10.1021/bi048253i.Peer-Reviewed Original ResearchMeSH KeywordsAdenine NucleotidesDEAD-box RNA HelicasesEscherichia coli ProteinsKineticsRNA HelicasesRNA-Binding ProteinsTemperatureThermodynamicsConceptsFluorescence resonance energy transferAbsence of RNARNA helicaseATP bindingNucleotide bindingConformational rearrangementsResonance energy transferConformational flexibilityDbpADependent conformationStructural rearrangementsDbpA.Protein AUnfavorable entropic contributionNucleotidesPhysiological temperatureBindingAssociation rate constantsADP