2010
Down-Regulation of a Host MicroRNA by a Herpesvirus saimiri Noncoding RNA
Cazalla D, Yario T, Steitz JA. Down-Regulation of a Host MicroRNA by a Herpesvirus saimiri Noncoding RNA. Science 2010, 328: 1563-1566. PMID: 20558719, PMCID: PMC3075239, DOI: 10.1126/science.1187197.Peer-Reviewed Original ResearchConceptsHSURs 1Noncoding RNAsHost cell gene expressionMiR-27Binding-dependent mannerPotential binding sitesMiRNA pathwayHost cell microRNAsCoimmunoprecipitation experimentsEctopic expressionTarget genesTransient knockdownGene expressionUnknown functionHost microRNAsViral strategiesDown regulationBinding sitesMiRNAsMicroRNAsRNAExpressionCellsT cellsNcRNA
2005
Molecular basis for RNA kink-turn recognition by the h15.5K small RNP protein
Szewczak LB, Gabrielsen JS, Degregorio SJ, Strobel SA, Steitz JA. Molecular basis for RNA kink-turn recognition by the h15.5K small RNP protein. RNA 2005, 11: 1407-1419. PMID: 16120832, PMCID: PMC1370824, DOI: 10.1261/rna.2830905.Peer-Reviewed Original ResearchConceptsMolecular basisRNA-protein complexesMobility shift assaysKink-turn motifPotential binding sitesNucleotide analog interference mappingSmall nucleolarSnoRNP assemblyRNA-RNA contactsRNP proteinsShift assaysSnoRNAsBackbone atomsBinding sitesPreferential bindingProteinEnergetic contributionsInterference mappingMinor interactionsStructural contextPotential sitesNucleolarSitesRNAMotif
2001
Internal Modification of U2 Small Nuclear (Snrna) Occurs in Nucleoli of Xenopus Oocytes
Yu Y, Shu M, Narayanan A, Terns R, Terns M, Steitz J. Internal Modification of U2 Small Nuclear (Snrna) Occurs in Nucleoli of Xenopus Oocytes. Journal Of Cell Biology 2001, 152: 1279-1288. PMID: 11257127, PMCID: PMC2199211, DOI: 10.1083/jcb.152.6.1279.Peer-Reviewed Original ResearchConceptsNucleolar localizationCajal bodiesU2 RNAInternal modificationSmall nuclearSm binding siteNucleolar localization signalSmall nucleolar RNAsXenopus oocytesCytoplasm of oocytesU2 small nuclearGuanosine capLocalization signalNucleolar RNAsRNAs showSubcellular sitesIntranuclear localizationIsolated nucleiRNABinding sitesNucleoliOocytesNucleotidesCytoplasmU2
1993
A general two-metal-ion mechanism for catalytic RNA.
Steitz TA, Steitz JA. A general two-metal-ion mechanism for catalytic RNA. Proceedings Of The National Academy Of Sciences Of The United States Of America 1993, 90: 6498-6502. PMID: 8341661, PMCID: PMC46959, DOI: 10.1073/pnas.90.14.6498.Peer-Reviewed Original ResearchConceptsMetal ionsTwo-metal-ion mechanismCatalytic metal ionPhosphoryl transfer reactionsChemical catalysisLewis acidTransfer reactionsReaction pathwaysTransition stateProtein enzymesCatalytic siteSugar hydroxylsIonsGroup I self-splicing intronCatalytic RNAReactionSelf-splicing intronsP hydrolysisCatalysisBinding sitesOxyanionsHydroxylSpecific binding sitesHydrolysisAcid
1991
An intact Box C sequence in the U3 snRNA is required for binding of fibrillarin, the protein common to the major family of nucleolar snRNPs.
Baserga SJ, Yang XD, Steitz JA. An intact Box C sequence in the U3 snRNA is required for binding of fibrillarin, the protein common to the major family of nucleolar snRNPs. The EMBO Journal 1991, 10: 2645-2651. PMID: 1714385, PMCID: PMC452965, DOI: 10.1002/j.1460-2075.1991.tb07807.x.Peer-Reviewed Original ResearchConceptsBox CU3 snRNANucleolar small RNAsSite-specific mutationsShort nucleotide sequencesFibrillarin proteinSmall RNAsDeletion analysisCommon binding siteBox DNucleotide sequenceSnRNPsMajor familiesSnRNAU3 snRNPRNAInput RNAFibrillarinBinding sitesC sequencesBindingProteinSequenceAnti-fibrillarin autoantibodiesBiogenesis