2022
The nucleoporin Gle1 activates DEAD-box protein 5 (Dbp5) by promoting ATP binding and accelerating rate limiting phosphate release
Gray S, Cao W, Montpetit B, De La Cruz EM. The nucleoporin Gle1 activates DEAD-box protein 5 (Dbp5) by promoting ATP binding and accelerating rate limiting phosphate release. Nucleic Acids Research 2022, 50: 3998-4011. PMID: 35286399, PMCID: PMC9023272, DOI: 10.1093/nar/gkac164.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesAdenosine TriphosphateDEAD-box RNA HelicasesNuclear Pore Complex ProteinsNucleocytoplasmic Transport ProteinsPhosphatesRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsConceptsNuclear pore complexRNA exportDEAD-box protein Dbp5ATPase cycleDbp5's ATPase activityDEAD (Asp-Glu-Ala-Asp) box protein 5Pore complexDbp5ATP bindingATPase cyclingNucleotide stateCytoplasmic faceGle1Pool of ATPADP-PiGene expressionProtein 5Mechanistic understandingNucleoporinsNup159ATPase activityATP dissociationATPPi releasePi release rate
2015
Pi Release Limits the Intrinsic and RNA-Stimulated ATPase Cycles of DEAD-Box Protein 5 (Dbp5)
Wong EV, Cao W, Vörös J, Merchant M, Modis Y, Hackney DD, Montpetit B, De La Cruz EM. Pi Release Limits the Intrinsic and RNA-Stimulated ATPase Cycles of DEAD-Box Protein 5 (Dbp5). Journal Of Molecular Biology 2015, 428: 492-508. PMID: 26730886, PMCID: PMC4744555, DOI: 10.1016/j.jmb.2015.12.018.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesDEAD-box RNA HelicasesKineticsNucleocytoplasmic Transport ProteinsPhosphatesRNASaccharomyces cerevisiaeSaccharomyces cerevisiae Proteins
2011
Cofilin Tunes the Nucleotide State of Actin Filaments and Severs at Bare and Decorated Segment Boundaries
Suarez C, Roland J, Boujemaa-Paterski R, Kang H, McCullough BR, Reymann AC, Guérin C, Martiel JL, De La Cruz EM, Blanchoin L. Cofilin Tunes the Nucleotide State of Actin Filaments and Severs at Bare and Decorated Segment Boundaries. Current Biology 2011, 21: 862-868. PMID: 21530260, PMCID: PMC3100394, DOI: 10.1016/j.cub.2011.03.064.Peer-Reviewed Original ResearchMechanism of Mss116 ATPase Reveals Functional Diversity of DEAD-Box Proteins
Cao W, Coman MM, Ding S, Henn A, Middleton ER, Bradley MJ, Rhoades E, Hackney DD, Pyle AM, De La Cruz EM. Mechanism of Mss116 ATPase Reveals Functional Diversity of DEAD-Box Proteins. Journal Of Molecular Biology 2011, 409: 399-414. PMID: 21501623, PMCID: PMC3125984, DOI: 10.1016/j.jmb.2011.04.004.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine DiphosphateAdenosine TriphosphatasesDEAD-box RNA HelicasesIntronsRNASaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsThermodynamicsConceptsGroup II intronsWeak RNARNA bindingDEAD-box RNA helicase proteinATP hydrolysisBiochemical intermediatesDEAD-box proteinsRNA helicase proteinStrong RNA bindingStable RNA duplexAbsence of nucleotideATP utilizationStrong thermodynamic couplingFunctional diversityIntron splicingStrong RNAIntron foldingVivo splicingHelicase proteinMRNA translationMss116ATPase cyclingVivo functionBiological roleADP state
2010
Structure-Based Analysis of Toxoplasma gondii Profilin: A Parasite-Specific Motif Is Required for Recognition by Toll-Like Receptor 11
Kucera K, Koblansky AA, Saunders LP, Frederick KB, De La Cruz EM, Ghosh S, Modis Y. Structure-Based Analysis of Toxoplasma gondii Profilin: A Parasite-Specific Motif Is Required for Recognition by Toll-Like Receptor 11. Journal Of Molecular Biology 2010, 403: 616-629. PMID: 20851125, PMCID: PMC2957522, DOI: 10.1016/j.jmb.2010.09.022.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceAnimalsBase SequenceCrystallography, X-RayDNA PrimersImmunity, InnateIn Vitro TechniquesMacrophages, PeritonealMiceMice, KnockoutModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedMutant ProteinsPlasmodium falciparumProfilinsProtein Structure, SecondaryProtozoan ProteinsRabbitsRecombinant ProteinsSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidSignal TransductionStatic ElectricityToll-Like ReceptorsToxoplasmaConceptsAcidic loopToll-like receptor 11Β-hairpinLong β-hairpinApicomplexan parasite Cryptosporidium parvumActin-binding surfaceFilament barbed endsStructure-based analysisYeast profilinGondii profilinProfilin mutantsGliding motilityParasite Cryptosporidium parvumT. gondii profilinNucleotide exchangeToxoplasma gondii profilinRabbit actinPlasmodium falciparum resultsActin polymerizationApicomplexan protozoaHomologous loopBarbed endsHost cellsIL-12 secretionInnate immune response
2009
Kinetic Analysis of the Guanine Nucleotide Exchange Activity of TRAPP, a Multimeric Ypt1p Exchange Factor
Chin HF, Cai Y, Menon S, Ferro-Novick S, Reinisch KM, De La Cruz EM. Kinetic Analysis of the Guanine Nucleotide Exchange Activity of TRAPP, a Multimeric Ypt1p Exchange Factor. Journal Of Molecular Biology 2009, 389: 275-288. PMID: 19361519, PMCID: PMC2770256, DOI: 10.1016/j.jmb.2009.03.068.Peer-Reviewed Original ResearchConceptsMembrane trafficExchange factorGuanine nucleotide exchange activityRab GTPase Ypt1pLarge multimeric assembliesNucleotide exchange activityThermodynamic linkage analysisWeak thermodynamic couplingTRAPP complexesStable ternary complexTRAPP subunitsGEF activityYpt1pNucleotide bindingMultimeric assembliesNucleotide exchangeNucleotide dissociationNucleotide affinityLinkage analysisIndependent pathwaysGEF systemTernary complexExchange activityTRAPPOverall net change
2008
The Structural Basis for Activation of the Rab Ypt1p by the TRAPP Membrane-Tethering Complexes
Cai Y, Chin HF, Lazarova D, Menon S, Fu C, Cai H, Sclafani A, Rodgers DW, De La Cruz EM, Ferro-Novick S, Reinisch KM. The Structural Basis for Activation of the Rab Ypt1p by the TRAPP Membrane-Tethering Complexes. Cell 2008, 133: 1202-1213. PMID: 18585354, PMCID: PMC2465810, DOI: 10.1016/j.cell.2008.04.049.Peer-Reviewed Original Research