2007
Solution Structure of an rRNA Substrate Bound to the Pseudouridylation Pocket of a Box H/ACA snoRNA
Jin H, Loria JP, Moore PB. Solution Structure of an rRNA Substrate Bound to the Pseudouridylation Pocket of a Box H/ACA snoRNA. Molecular Cell 2007, 26: 205-215. PMID: 17466623, DOI: 10.1016/j.molcel.2007.03.014.Peer-Reviewed Original ResearchConceptsPseudouridylation pocketBox H/ACA small nucleolar ribonucleoproteinsBox H/ACA snoRNAsSubstrate sequenceSmall nucleolar ribonucleoproteinSolution structureInteraction motifsNucleolar ribonucleoproteinSpecific uridinesRNA componentRRNA substrateRRNA sequencesSnoRNAsSequencePocketComplexesPseudouridylationSnoRNPsRibonucleoproteinHJ1RNAMotifInteractsStrandsUridine
2005
Gene replacement in Haloarcula marismortui: construction of a strain with two of its three chromosomal rRNA operons deleted
Tu D, Blaha G, Moore PB, Steitz TA. Gene replacement in Haloarcula marismortui: construction of a strain with two of its three chromosomal rRNA operons deleted. Extremophiles 2005, 9: 427-435. PMID: 15970993, DOI: 10.1007/s00792-005-0459-y.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceBlotting, SouthernChromosome MappingCrystallography, X-RayDNADNA PrimersElectronsEscherichia coli ProteinsGene DeletionGenetic TechniquesHaloarcula marismortuiModels, ChemicalModels, GeneticModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedMutationOperonPlasmidsReverse Transcriptase Polymerase Chain ReactionRibosomal ProteinsRNA-Binding ProteinsRNA, RibosomalRNA, Ribosomal, 23SRRNA OperonSucroseConceptsRRNA operonsHaloarcula marismortuiChromosomal rRNA operonsLarge ribosomal subunitRibosomal protein L22Wild-type organismsSite-directed mutagenesisAmino acid deletionBacteriorhodopsin geneRrnB operonProtein L22Ribosomal subunitRRNA geneGene replacementOperonWild typeRich mediumAcid deletionSuch mutationsGenesHalobacterium halobiumStructural consequencesMarismortuiAtomic resolutionStrains
2004
The contribution of metal ions to the structural stability of the large ribosomal subunit
Klein DJ, Moore PB, Steitz TA. The contribution of metal ions to the structural stability of the large ribosomal subunit. RNA 2004, 10: 1366-1379. PMID: 15317974, PMCID: PMC1370624, DOI: 10.1261/rna.7390804.Peer-Reviewed Original ResearchConceptsLarge ribosomal subunitRibosomal subunitMonovalent cation binding siteNucleotide basesSpecific RNA structuresPeptidyl transferase centerLarge RNA moleculesPhylogenetic kingdomsRibosomal proteinsAppearance of proteinsRRNA structureHaloarcula marismortuiMajor groove sideEvolutionary periodRNA moleculesRNA structureCation binding siteStructural domainsTertiary structureProtein groupsMonovalent cationsBinding sitesRRNAGroove sideSubunitsThe structure of a ribosomal protein S8/spc operon mRNA complex
Merianos HJ, Wang J, Moore PB. The structure of a ribosomal protein S8/spc operon mRNA complex. RNA 2004, 10: 954-964. PMID: 15146079, PMCID: PMC1370587, DOI: 10.1261/rna.7030704.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceBinding SitesCrystallography, X-RayEscherichia coliEscherichia coli ProteinsGenes, BacterialLigandsMacromolecular SubstancesModels, MolecularNucleic Acid ConformationOperonProtein BiosynthesisRibosomal ProteinsRNA, BacterialRNA, MessengerSpecies SpecificityStatic ElectricityConceptsSpc operon mRNAOperon mRNARibosomal protein cistronsSmall ribosomal subunitRibosomal initiation complexResolution crystal structureProtein synthesis resultsSpc operonAutogenous regulationTranslational repressionInitiation complexOwn mRNARibosomal subunitS8 bindingSequence differencesCistronInternal sequencesMRNAGenesConformational similarityBindingComplexesRetroregulationRRNAsOperon
2002
The Structures of Four Macrolide Antibiotics Bound to the Large Ribosomal Subunit
Hansen JL, Ippolito JA, Ban N, Nissen P, Moore PB, Steitz TA. The Structures of Four Macrolide Antibiotics Bound to the Large Ribosomal Subunit. Molecular Cell 2002, 10: 117-128. PMID: 12150912, DOI: 10.1016/s1097-2765(02)00570-1.Peer-Reviewed Original Research