2009
Structures of Triacetyloleandomycin and Mycalamide A Bind to the Large Ribosomal Subunit of Haloarcula marismortuiâ–¿
Gürel G, Blaha G, Steitz TA, Moore PB. Structures of Triacetyloleandomycin and Mycalamide A Bind to the Large Ribosomal Subunit of Haloarcula marismortui▿. Antimicrobial Agents And Chemotherapy 2009, 53: 5010-5014. PMID: 19738021, PMCID: PMC2786347, DOI: 10.1128/aac.00817-09.Peer-Reviewed Original Research
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, RibosomalRNA, Ribosomal, 23SRNA-Binding ProteinsrRNA 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 sideSubunits