2016
Host miRNA degradation by Herpesvirus saimiri small nuclear RNA requires an unstructured interacting region
Pawlica P, Moss WN, Steitz JA. Host miRNA degradation by Herpesvirus saimiri small nuclear RNA requires an unstructured interacting region. RNA 2016, 22: 1181-1189. PMID: 27335146, PMCID: PMC4931111, DOI: 10.1261/rna.054817.115.Peer-Reviewed Original ResearchConceptsSmall nuclear RNAMiR-27Nuclear RNAVivo secondary structureBioinformatic structural analysisBinding site sequenceMiRNA degradationU RNARNA functionMutagenic analysisHSUR1Interacting regionsSite sequenceHost microRNAsSecondary structureHerpesvirus saimiriT cell activationOncogenic herpesvirusRNAStructural flexibilityDecreased levelsMutantsStructural analysisDegradationMicroRNAs
2010
Poly(A) Tail Recognition by a Viral RNA Element Through Assembly of a Triple Helix
Mitton-Fry RM, DeGregorio SJ, Wang J, Steitz TA, Steitz JA. Poly(A) Tail Recognition by a Viral RNA Element Through Assembly of a Triple Helix. Science 2010, 330: 1244-1247. PMID: 21109672, PMCID: PMC3074936, DOI: 10.1126/science.1195858.Peer-Reviewed Original ResearchConceptsSarcoma-associated herpesvirusBox H/ACA small nucleolar RNAsMajor-groove triple helixNuclear noncoding RNANuclear retention elementSmall nucleolar RNAsViral RNA elementsRich internal loopTriple helixKaposi's sarcoma-associated herpesvirusPAN RNADeadenylation assaysRNA decayRNA clampNucleolar RNAsNoncoding RNAsNuclear RNATail recognitionRNA elementsFunctional importanceAngstrom resolutionRich loopSecondary structureRNAEne core
2008
Flexibility in the site of exon junction complex deposition revealed by functional group and RNA secondary structure alterations in the splicing substrate
Mishler DM, Christ AB, Steitz JA. Flexibility in the site of exon junction complex deposition revealed by functional group and RNA secondary structure alterations in the splicing substrate. RNA 2008, 14: 2657-2670. PMID: 18952819, PMCID: PMC2590960, DOI: 10.1261/rna.1312808.Peer-Reviewed Original ResearchConceptsExon junction complexRNA secondary structureEJC depositionSplicing substrateMammalian nonsense-mediated mRNA decayNonsense-mediated mRNA decaySecondary structureStretches of DNATranslational regulationMRNA decayCoimmunoprecipitation assaysJunction complexSecondary structure alterationsDNA nucleotidesStructure alterationsH protectionUpstream shiftToeprintingExonsSitesNucleotidesDNACrystal structureDeposition sitesMRNA
1996
More Sm snRNAs from Vertebrate Cells
Yu Y, Tarn W, Yario T, Steitz J. More Sm snRNAs from Vertebrate Cells. Experimental Cell Research 1996, 229: 276-281. PMID: 8986610, DOI: 10.1006/excr.1996.0372.Peer-Reviewed Original Research
1988
Trans splicing involves a novel form of small nuclear ribonucleoprotein particles
Bruzik J, Doren K, Hirsh D, Steitz J. Trans splicing involves a novel form of small nuclear ribonucleoprotein particles. Nature 1988, 335: 559-562. PMID: 2971142, DOI: 10.1038/335559a0.Peer-Reviewed Original ResearchConceptsSmall nuclear ribonucleoproteinSL RNACis splicingSplice siteNuclear ribonucleoproteinPrecursor-messenger RNA (pre-mRNA) transcriptsHeLa cell nuclear extractsSame nuclear compartmentTrans-splicing reactionCell nuclear extractsPossible secondary structuresMessenger RNA transcriptsSm snRNPSplice acceptor siteTrans splicingCellular machineryLeader transcriptNuclear compartmentNucleotide sequenceSplicing processRNA transcriptsNuclear extractsSnRNPSplicingSecondary structure
1987
Structural Analysis of the Human U3 Ribonucleoprotein Particle Reveal a Conserved Sequence Available for Base Pairing with Pre-rRna
Parker K, Steitz J. Structural Analysis of the Human U3 Ribonucleoprotein Particle Reveal a Conserved Sequence Available for Base Pairing with Pre-rRna. Molecular And Cellular Biology 1987, 7: 2899-2913. DOI: 10.1128/mcb.7.8.2899-2913.1987.Peer-Reviewed Original ResearchProtein-RNA interactionsSecondary structureSubsequent reverse transcriptionRNA secondary structureHuman U3Phosphorylated proteinsConserved sequencesProcessing eventsPre-rRNAAlternative functionsBase pairsNucleotides -159Specific nucleasesHeLa cellsProtein constituentsRNase ABase pairingRNPProteinNonphosphorylated proteinsRRNAReverse transcriptionSequenceKilodaltonsNucleotides 65Structural analysis of the human U3 ribonucleoprotein particle reveal a conserved sequence available for base pairing with pre-rRNA.
Parker KA, Steitz JA. Structural analysis of the human U3 ribonucleoprotein particle reveal a conserved sequence available for base pairing with pre-rRNA. Molecular And Cellular Biology 1987, 7: 2899-2913. PMID: 2959855, PMCID: PMC367909, DOI: 10.1128/mcb.7.8.2899.Peer-Reviewed Original ResearchConceptsProtein-RNA interactionsSecondary structureSubsequent reverse transcriptionRNA secondary structureHuman U3Phosphorylated proteinsRibonucleoprotein particleProcessing eventsAlternative functionsBase pairsNucleotides -159Specific nucleasesHeLa cellsProtein constituentsRNase ARNPProteinNonphosphorylated proteinsRRNAReverse transcriptionSequenceKilodaltonsNucleotides 65Specific reagentsTranscription
1981
Sequence of U1 RNA from Drosophila melanogaster: implications for U1 secondary structure and possible involvement in splicing
Mount S, Steitz J. Sequence of U1 RNA from Drosophila melanogaster: implications for U1 secondary structure and possible involvement in splicing. Nucleic Acids Research 1981, 9: 6351-6368. PMID: 6172778, PMCID: PMC327608, DOI: 10.1093/nar/9.23.6351.Peer-Reviewed Original ResearchConceptsU1 RNAU1 sequenceCultured Drosophila melanogaster cellsDrosophila U1 RNAU1 RNA sequenceDrosophila melanogaster cellsHuman U1 RNASecondary structure modelDNA sequence determinationDonor splice junctionGenomic clonesDrosophila melanogasterSplicing reactionRNA moleculesU1 snRNPsConsensus sequenceSplice junctionsRNA sequencesNucleotides 3Sequence determinationSecondary structureRNASplicingMolecular interactionsSequence
1974
High resolution proton NMR study of an isolated fragment of R17 bacteriophage mRNA
HILBERS CW, SHULMAN RG, YAMANE T, STEITZ JA. High resolution proton NMR study of an isolated fragment of R17 bacteriophage mRNA. Nature 1974, 248: 225-226. PMID: 4819416, DOI: 10.1038/248225a0.Peer-Reviewed Original ResearchConceptsHelical regionBase pairsBase pairingWatson-Crick base pairingIsolated fragmentsSecondary structureNMR spectraModel systemNuclear magnetic resonance spectraHigh-resolution nuclear magnetic resonance spectraNucleic acidsHydrogen-bonded protonsMagnetic resonance spectraProton NMR studiesAdjacent basesLeaf modelFragmentsNH protonsNMR studiesTRNAResonance spectraHigh-resolution proton NMR studiesHelixPairingGuanine