2025
Structure and evolution of photosystem I in the early-branching cyanobacterium Anthocerotibacter panamensis
Jiang H, Gisriel C, Cardona T, Flesher D, Brudvig G, Ho M. Structure and evolution of photosystem I in the early-branching cyanobacterium Anthocerotibacter panamensis. Proceedings Of The National Academy Of Sciences Of The United States Of America 2025, 122: e2427090122. PMID: 40366692, PMCID: PMC12107172, DOI: 10.1073/pnas.2427090122.Peer-Reviewed Original ResearchConceptsPhotosystem IAnalysis of photosystem IEvolution of Photosystem IEvolution of photosynthesisAncestor of cyanobacteriaCryo-EM structureAncestral traitPhylogenetic analysisPhotosynthesis evolutionSequence levelPhotosynthesis studiesBiochemical characterizationOxygenic photosynthesisOligomeric formsPhotosynthesisCyanobacteriaCarotenoid compositionSubunit compositionGenusCyanobacteriumAncestorSubunitSequenceIsolatesEvolution
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
1999
A dimer of the lymphoid protein RAG1 recognizes the recombination signal sequence and the complex stably incorporates the high mobility group protein HMG2
Rodgers K, Villey I, Ptaszek L, Corbett E, Schatz D, Coleman J. A dimer of the lymphoid protein RAG1 recognizes the recombination signal sequence and the complex stably incorporates the high mobility group protein HMG2. Nucleic Acids Research 1999, 27: 2938-2946. PMID: 10390537, PMCID: PMC148510, DOI: 10.1093/nar/27.14.2938.Peer-Reviewed Original ResearchConceptsRecombination signal sequencesSignal sequenceCore RAG1RAG1/RAG2 complexAbsence of RAG2Lymphoid-specific proteinsElectrophoretic mobility shift assaysSingle recombination signal sequencesMobility shift assaysRAG1 proteinProteins RAG1DNA sequencesMinimal speciesShift assaysOligomeric complexesHeptamer sequenceCompetition assaysRAG1Escherichia coliOligomeric formsRAG2Cleavage activityHMG2ProteinJ region
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