2018
Nup159 Weakens Gle1 Binding to Dbp5 But Does Not Accelerate ADP Release
Wong EV, Gray S, Cao W, Montpetit R, Montpetit B, De La Cruz EM. Nup159 Weakens Gle1 Binding to Dbp5 But Does Not Accelerate ADP Release. Journal Of Molecular Biology 2018, 430: 2080-2095. PMID: 29782832, PMCID: PMC6003625, DOI: 10.1016/j.jmb.2018.05.025.Peer-Reviewed Original ResearchConceptsEssential DEAD-box proteinADP releaseDbp5's ATPase activityDEAD-box proteinsNucleotide exchange factorsDbp5 activityMRNA exportRNA metabolismExchange factorDbp5Cellular processesATPase cyclingNup159Gle1ATP affinityMechanochemical cycleATPase activityADPATP releaseDDX19NTPasesNucleoporinsDetailed characterizationRNARegulator
2012
ATP Utilization and RNA Conformational Rearrangement by DEAD-Box Proteins
Henn A, Bradley MJ, De La Cruz EM. ATP Utilization and RNA Conformational Rearrangement by DEAD-Box Proteins. Annual Review Of Biophysics 2012, 41: 247-267. PMID: 22404686, PMCID: PMC7761782, DOI: 10.1146/annurev-biophys-050511-102243.Peer-Reviewed Original ResearchConceptsDEAD-box proteinsNucleotide-dependent interactionRegulatory partner proteinsMolecular motor proteinsMolecular motor functionPartner proteinsRNA helicasesHelicase coreRNA helicaseRNA metabolismVivo foldingATP bindingDBP functionMotor proteinsCellular RNARNA structureQuantitative mechanistic understandingConformational rearrangementsBiophysical investigationsEnzymatic adaptationLarge familyMechanistic understandingProteinRNAAuxiliary domainChapter Two Analyzing ATP Utilization by DEAD-Box RNA Helicases Using Kinetic and Equilibrium Methods
Bradley MJ, De La Cruz EM. Chapter Two Analyzing ATP Utilization by DEAD-Box RNA Helicases Using Kinetic and Equilibrium Methods. Methods In Enzymology 2012, 511: 29-63. PMID: 22713314, PMCID: PMC7768905, DOI: 10.1016/b978-0-12-396546-2.00002-4.Peer-Reviewed Original ResearchConceptsDEAD-box RNA helicasesProduct release rate constantsEscherichia coli DbpAATP utilizationSteady-state ATPase activityRNA unwindingRNA helicasesATP bindingPreferred kinetic pathwayDsRNA unwindingConformational rearrangementsATPase activityRNAUnwindingCombination of equilibriumMss116HelicasesDbpAChapter TwoSubstrate propertiesSolution conditionsPathwayBindingKinetic pathwaysRearrangement
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