2022
Uncovering translation roadblocks during the development of a synthetic tRNA
Prabhakar A, Krahn N, Zhang J, Vargas-Rodriguez O, Krupkin M, Fu Z, Acosta-Reyes FJ, Ge X, Choi J, Crnković A, Ehrenberg M, Puglisi EV, Söll D, Puglisi J. Uncovering translation roadblocks during the development of a synthetic tRNA. Nucleic Acids Research 2022, 50: 10201-10211. PMID: 35882385, PMCID: PMC9561287, DOI: 10.1093/nar/gkac576.Peer-Reviewed Original ResearchConceptsOrthogonal translation systemGenetic code expansionCode expansionTertiary interactionsNon-canonical amino acidsAminoacyl-tRNA substratesDomains of lifeAminoacyl-tRNA synthetaseTranslation systemSingle nucleotide mutationsSingle-molecule fluorescenceDistinct tRNAsNon-canonical structuresSelenocysteine insertionRibosomal translationTRNARibosomesSynthetic tRNANucleotide mutationsAmino acidsSame organismP siteOrganismsTranslocationTranslation
2015
Structural Analysis of Multi-Helical RNAs by NMR–SAXS/WAXS: Application to the U4/U6 di-snRNA
Cornilescu G, Didychuk A, Rodgers M, Michael L, Burke J, Montemayor E, Hoskins A, Butcher S. Structural Analysis of Multi-Helical RNAs by NMR–SAXS/WAXS: Application to the U4/U6 di-snRNA. Journal Of Molecular Biology 2015, 428: 777-789. PMID: 26655855, PMCID: PMC4790120, DOI: 10.1016/j.jmb.2015.11.026.Peer-Reviewed Original ResearchConceptsU4/U6 di-snRNAScattering dataTri-snRNPAnalysis of RNA structureCryo-electron microscopy structureResonance energy transfer dataX-ray scattering dataMagnetic susceptibility anisotropyRNA structureAssembled spliceosomeRibonucleoprotein complexTertiary interactionsU4/U6Energy transfer dataAlignment mediaSusceptibility anisotropyCryo-electronAlignment tensorStructural investigationsRNAX-rayNucleic acidsStructural analysisWAXS dataY-shaped structure
2010
Inclusion of weak high-resolution X-ray data for improvement of a group II intron structure
Wang J. Inclusion of weak high-resolution X-ray data for improvement of a group II intron structure. Acta Crystallographica Section D, Structural Biology 2010, 66: 988-1000. PMID: 20823550, DOI: 10.1107/s0907444910029938.Peer-Reviewed Original Research
2009
Tertiary architecture of the Oceanobacillus iheyensis group II intron
Toor N, Keating KS, Fedorova O, Rajashankar K, Wang J, Pyle AM. Tertiary architecture of the Oceanobacillus iheyensis group II intron. RNA 2009, 16: 57-69. PMID: 19952115, PMCID: PMC2802037, DOI: 10.1261/rna.1844010.Peer-Reviewed Original ResearchConceptsGroup II intronsPotential evolutionary relationshipsGroup II intron structureGroup IIC intronIntron structureEvolutionary relationshipsEukaryotic spliceosomeInteraction networksRNA moleculesIntronsTertiary structural organizationGenetic studiesRibose zipperRNA foldingTertiary interactionsLarge ribozymesInteraction nodesStructural organizationTertiary architectureEukaryotesSpliceosomeGene therapyGenomeZipperFolding
2008
A relaxed active site after exon ligation by the group I intron
Lipchock SV, Strobel SA. A relaxed active site after exon ligation by the group I intron. Proceedings Of The National Academy Of Sciences Of The United States Of America 2008, 105: 5699-5704. PMID: 18408159, PMCID: PMC2311373, DOI: 10.1073/pnas.0712016105.Peer-Reviewed Original ResearchConceptsActive siteMetal ionsRelaxed active siteActive site metal ionScissile phosphateDirect metal coordinationHydrogen bonding contactsMetal coordinationBonding contactsTransition stateCrystal structureThermodynamic measurementsIonsGround stateStructureCoordinationStructural observationsTertiary interactionsIntron releaseExon ligationGroup I intronPhosphateComplexesReactionSecond step
2004
Prediction of functional tertiary interactions and intermolecular interfaces from primary sequence data
Pang PS, Jankowsky E, Wadley LM, Pyle AM. Prediction of functional tertiary interactions and intermolecular interfaces from primary sequence data. Journal Of Experimental Zoology Part B Molecular And Developmental Evolution 2004, 304B: 50-63. PMID: 15595717, DOI: 10.1002/jez.b.21024.Peer-Reviewed Original ResearchConceptsRNA-protein complexesPattern of conservationProtein-protein interactionsPrimary sequence dataRNA-proteinDifferent organismsSequence dataSequence informationIntermolecular interfaceEnergetic couplingTertiary interactionsMacromolecular interactionsRNAsGenesImportant intramolecular interactionsProteinSequenceIntramolecular interactionsRNAOrganismsSpeciesInteractionMutationsNumber of predictionsConservation
1999
Nucleotide Analog Interference Mapping of the Hairpin Ribozyme: Implications for Secondary and Tertiary Structure Formation
Ryder S, Strobel S. Nucleotide Analog Interference Mapping of the Hairpin Ribozyme: Implications for Secondary and Tertiary Structure Formation. Journal Of Molecular Biology 1999, 291: 295-311. PMID: 10438622, DOI: 10.1006/jmbi.1999.2959.Peer-Reviewed Original ResearchConceptsNucleotide analog interference mappingLoop AMinor groove edgeTertiary structure formationProper foldingThree-dimensional structureHairpin ribozymeNucleotide conservationNMR structureLoop BInterference mappingTertiary interactionsLoop B.Purine nucleotidesBiochemical evidenceRibozymeIntact ribozyme
1990
Direct measurement of oligonucleotide substrate binding to wild-type and mutant ribozymes from Tetrahymena.
Pyle AM, McSwiggen JA, Cech TR. Direct measurement of oligonucleotide substrate binding to wild-type and mutant ribozymes from Tetrahymena. Proceedings Of The National Academy Of Sciences Of The United States Of America 1990, 87: 8187-8191. PMID: 2236030, PMCID: PMC54920, DOI: 10.1073/pnas.87.21.8187.Peer-Reviewed Original ResearchConceptsSingle base changeBase-pairing interactionsGuanosine-binding siteRNA substratesSubstrate bindingRNA cleavageOligonucleotide substratesEfficient RNA cleavageTertiary interactionsBase changesRibozyme variantsTetrahymena ribozymeWeak substrateMutant ribozymesRibozymePolyacrylamide gelsEquilibrium dissociation constantsDeoxyribose sugarCatalytic activityDivalent cationsEnergetic stabilizationMutagenesisDissociation constantsTetrahymenaLow Mg2
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