2015
Herpesvirus saimiri MicroRNAs Preferentially Target Host Cell Cycle Regulators
Guo YE, Oei T, Steitz JA. Herpesvirus saimiri MicroRNAs Preferentially Target Host Cell Cycle Regulators. Journal Of Virology 2015, 89: 10901-10911. PMID: 26292323, PMCID: PMC4621106, DOI: 10.1128/jvi.01884-15.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBinding SitesBlotting, WesternCallithrixCDC2 Protein KinaseCell Cycle ProteinsEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsHEK293 CellsHerpesvirus 2, SaimiriineHigh-Throughput Nucleotide SequencingHumansImmunoprecipitationLuciferasesMicroRNAsPhosphorylationRNA, MessengerT-LymphocytesConceptsHost cell cycle regulatorsViral miRNAsCell cycle regulatorsHerpesvirus saimiriMRNA targetsCycle regulatorsProtein-coding genesPre-miRNA hairpinsCross-linking immunoprecipitationGene ontology analysisHigh-throughput sequencingOpen reading frameOncogenic Herpesvirus saimiriCyclin-dependent kinasesP300 transcriptional coactivatorCell cycle progressionKey negative regulatorMarmoset T cellsHITS-CLIPRepresses expressionOntology analysisTranscriptional coactivatorViral life cyclePrimary transcriptCellular transformation
2010
miR-29 and miR-30 regulate B-Myb expression during cellular senescence
Martinez I, Cazalla D, Almstead LL, Steitz JA, DiMaio D. miR-29 and miR-30 regulate B-Myb expression during cellular senescence. Proceedings Of The National Academy Of Sciences Of The United States Of America 2010, 108: 522-527. PMID: 21187425, PMCID: PMC3021067, DOI: 10.1073/pnas.1017346108.Peer-Reviewed Original ResearchConceptsB-myb expressionCellular senescenceMiR-30MiR-29Reporter constructsEndogenous B-MybMajor tumor suppressor mechanismTumor suppressor mechanismIrreversible growth arrestMicroRNA familiesMutant 3'UTRCellular DNA synthesisB-MybReplicative senescenceCompensatory mutationsGrowth arrestMutant sitesRb pathwaySenescenceSuppressor mechanismDNA synthesisRepressionInhibits senescenceExpressionMutationsDown-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
2006
Multiple domains of EBER 1, an Epstein-Barr virus noncoding RNA, recruit human ribosomal protein L22
Fok V, Mitton-Fry RM, Grech A, Steitz JA. Multiple domains of EBER 1, an Epstein-Barr virus noncoding RNA, recruit human ribosomal protein L22. RNA 2006, 12: 872-882. PMID: 16556938, PMCID: PMC1440895, DOI: 10.1261/rna.2339606.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesCarrier ProteinsCell LineCross-Linking ReagentsElectrophoretic Mobility Shift AssayHerpesvirus 4, HumanHumansIn Vitro TechniquesMaltose-Binding ProteinsNucleic Acid ConformationPlasmidsProtein BindingProtein Structure, TertiaryRecombinant Fusion ProteinsRibosomal ProteinsRNA, UntranslatedRNA, ViralRNA-Binding ProteinsSequence DeletionTranscription, GeneticTransfectionUltraviolet RaysIn vivo assembly of functional U7 snRNP requires RNA backbone flexibility within the Sm-binding site
Kolev NG, Steitz JA. In vivo assembly of functional U7 snRNP requires RNA backbone flexibility within the Sm-binding site. Nature Structural & Molecular Biology 2006, 13: 347-353. PMID: 16547514, DOI: 10.1038/nsmb1075.Peer-Reviewed Original Research
2000
Protein Ligands to Hur Modulate Its Interaction with Target Mrnas in Vivo
Brennan C, Gallouzi I, Steitz J. Protein Ligands to Hur Modulate Its Interaction with Target Mrnas in Vivo. Journal Of Cell Biology 2000, 151: 1-14. PMID: 11018049, PMCID: PMC2189805, DOI: 10.1083/jcb.151.1.1.Peer-Reviewed Original ResearchMeSH KeywordsActive Transport, Cell NucleusAmino Acid SequenceAntigens, SurfaceBinding SitesCarrier ProteinsChromatography, AffinityCytoplasmELAV ProteinsELAV-Like Protein 1Fatty Acids, UnsaturatedHeLa CellsHumansKaryopherinsLigandsMolecular Sequence DataNeuropeptidesNuclear ProteinsPhosphoprotein PhosphatasesPhosphoproteinsProtein BindingProtein Phosphatase 2Protein TransportReceptors, Cytoplasmic and NuclearRNA StabilityRNA-Binding ProteinsRNA, MessengerSequence Analysis, ProteinConceptsAU-rich elementsTarget mRNAsStability of ARENuclear export factor CRM1Protein phosphatase 2A inhibitorExport factor CRM1Phosphatase 2A inhibitorCOOH-terminal tailInhibition of CRM1Leucine-rich repeatsC-fos geneMammalian proteinsLeptomycin BELAV familyCellular mRNAsNuclear retentionSecond motifHuR associationUntranslated regionBind regionsCytoplasmic distributionPp32Protein ligandsCRM1Terminal region
1997
The position of site-directed cleavage of RNA using RNase H and 2'-O-methyl oligonucleotides is dependent on the enzyme source.
Lapham J, Yu YT, Shu MD, Steitz JA, Crothers DM. The position of site-directed cleavage of RNA using RNase H and 2'-O-methyl oligonucleotides is dependent on the enzyme source. RNA 1997, 3: 950-1. PMID: 9292493, PMCID: PMC1369540.Peer-Reviewed Original ResearchSite-specific crosslinking of mammalian U11 and U6atac to the 5′ splice site of an AT–AC intron
Yu Y, Steitz J. Site-specific crosslinking of mammalian U11 and U6atac to the 5′ splice site of an AT–AC intron. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 6030-6035. PMID: 9177163, PMCID: PMC20995, DOI: 10.1073/pnas.94.12.6030.Peer-Reviewed Original ResearchPre-mRNA splicing: the discovery of a new spliceosome doubles the challenge
Tarn W, Steitz J. Pre-mRNA splicing: the discovery of a new spliceosome doubles the challenge. Trends In Biochemical Sciences 1997, 22: 132-137. PMID: 9149533, DOI: 10.1016/s0968-0004(97)01018-9.Peer-Reviewed Original Research
1995
Decreasing the distance between the two conserved sequence elements of histone pre-messenger RNA interferes with 3' processing in vitro.
Cho DC, Scharl EC, Steitz JA. Decreasing the distance between the two conserved sequence elements of histone pre-messenger RNA interferes with 3' processing in vitro. RNA 1995, 1: 905-14. PMID: 8548655, PMCID: PMC1369339.Peer-Reviewed Original ResearchAnimalsBase SequenceBinding SitesConserved SequenceHistonesMolecular Sequence DataMRNA Cleavage and Polyadenylation FactorsNuclear ProteinsNucleic Acid ConformationRibonucleoproteins, Small NuclearRNA PrecursorsRNA Processing, Post-TranscriptionalRNA-Binding ProteinsRNA, MessengerSequence DeletionSubstrate SpecificityTranscription, GeneticSite‐specific crosslinking of 4‐thiouridine‐modified human tRNA(3Lys) to reverse transcriptase from human immunodeficiency virus type I.
Mishima Y, Steitz JA. Site‐specific crosslinking of 4‐thiouridine‐modified human tRNA(3Lys) to reverse transcriptase from human immunodeficiency virus type I. The EMBO Journal 1995, 14: 2679-2687. PMID: 7540137, PMCID: PMC398382, DOI: 10.1002/j.1460-2075.1995.tb07266.x.Peer-Reviewed Original Research
1993
The U5 and U6 Small Nuclear RNAs as Active Site Components of the Spliceosome
Sontheimer E, Steitz J. The U5 and U6 Small Nuclear RNAs as Active Site Components of the Spliceosome. Science 1993, 262: 1989-1996. PMID: 8266094, DOI: 10.1126/science.8266094.Peer-Reviewed Original ResearchConceptsSmall nuclear RNANuclear RNAPrecursor messenger RNA splicingLariat intermediateU6 small nuclear RNAMessenger RNA splicingExon 1Self-splicing intronsActive site componentsRNA splicingMammalian spliceosomeU6 RNARNA contactsMechanistic parallelsPre-mRNAVitro splicingSubsequent splicingSplicingSpliceosomeSplice siteLast residueFirst residueFunctional interactionIntron productsRNAAssociation with terminal exons in pre-mRNAs: a new role for the U1 snRNP?
Wassarman KM, Steitz JA. Association with terminal exons in pre-mRNAs: a new role for the U1 snRNP? Genes & Development 1993, 7: 647-659. PMID: 8384583, DOI: 10.1101/gad.7.4.647.Peer-Reviewed Original ResearchAdenoviridaeBase SequenceBinding SitesCross-Linking ReagentsDNA Mutational AnalysisExonsFurocoumarinsHeLa CellsHistonesHumansMolecular Sequence DataOligonucleotide ProbesPoly ARestriction MappingRibonucleoprotein, U1 Small NuclearRNA PrecursorsRNA Processing, Post-TranscriptionalRNA SplicingRNA, Small NuclearSimian virus 40The cellular RNA-binding protein EAP recognizes a conserved stem-loop in the Epstein-Barr virus small RNA EBER 1.
Toczyski DP, Steitz JA. The cellular RNA-binding protein EAP recognizes a conserved stem-loop in the Epstein-Barr virus small RNA EBER 1. Molecular And Cellular Biology 1993, 13: 703-710. PMID: 8380232, PMCID: PMC358948, DOI: 10.1128/mcb.13.1.703.Peer-Reviewed Original ResearchConceptsCellular RNA-binding proteinsRNA-binding proteinDetailed mutational analysisStem-loop structureSequence-specific mannerRNase protection experimentsEpstein‐Barr virus small RNA EBER‐1Double-stranded regionsSmall RNAsDeletion mutantsEBER-1Mutational analysisFusion proteinProtection experimentsViral proteinsProteinRNAEpstein-Barr virusBindingMutantsHerpesvirus papioNucleotidesHairpinAntibodiesCells
1992
Viral small nuclear ribonucleoproteins bind a protein implicated in messenger RNA destabilization.
Myer VE, Lee SI, Steitz JA. Viral small nuclear ribonucleoproteins bind a protein implicated in messenger RNA destabilization. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 1296-1300. PMID: 1311093, PMCID: PMC48436, DOI: 10.1073/pnas.89.4.1296.Peer-Reviewed Original ResearchConceptsSmall nuclear ribonucleoproteinNuclear ribonucleoproteinCertain cellular mRNAsMessenger RNA destabilizationHerpesvirus saimiriNumber of protooncogenesHSUR 1HSURs 1Rapid degradationSmall RNAsU RNARNA destabilizationCellular mRNAsMarmoset T lymphocytesAbundant viral transcriptHost proteinsUntranslated regionAUUUA motifsExhibit sequencesViral transcriptsPrimate virusesViral transformationUnstable messagesProteinRibonucleoprotein
1987
Both conserved signals on mammalian histone pre-mRNAs associate with small nuclear ribonucleoproteins during 3' end formation in vitro.
Mowry KL, Steitz JA. Both conserved signals on mammalian histone pre-mRNAs associate with small nuclear ribonucleoproteins during 3' end formation in vitro. Molecular And Cellular Biology 1987, 7: 1663-1672. PMID: 2955216, PMCID: PMC365266, DOI: 10.1128/mcb.7.5.1663.Peer-Reviewed Original ResearchConceptsSmall nuclear ribonucleoproteinEnd formationNuclear ribonucleoproteinSequence elementsSm small nuclear ribonucleoproteinsMouse histone genesHeLa cell nuclear extractsHistone H3 transcriptsHuman histone H3Trimethylguanosine cap structureCell nuclear extractsHistone pre-mRNAHairpin loop structureH3 transcriptsHistone genesMammalian histonesU RNAHistone H3MRNA substratesPre-mRNACap structureMRNA associatesNuclear extractsRNA fragmentsProcessing reactions
1985
The 3′ Splice Site of Pre-Messenger RNA Is Recognized by a Small Nuclear Ribonucleoprotein
Chabot B, Black D, LeMaster D, Steitz J. The 3′ Splice Site of Pre-Messenger RNA Is Recognized by a Small Nuclear Ribonucleoprotein. Science 1985, 230: 1344-1349. PMID: 2933810, DOI: 10.1126/science.2933810.Peer-Reviewed Original Research
1979
Binding of mammalian ribosomes to ms2 phage rna reveals an overlapping gene encoding a lysis function
Atkins J, Steitz J, Anderson C, Model P. Binding of mammalian ribosomes to ms2 phage rna reveals an overlapping gene encoding a lysis function. Cell 1979, 18: 247-256. PMID: 498271, DOI: 10.1016/0092-8674(79)90044-8.Peer-Reviewed Original ResearchConceptsMammalian ribosomesLysis functionE. coli cell-free systemAmino acid polypeptideCoat protein geneAmino acid sequence analysisPartial amino acid sequence analysisMS2 phage RNAAcid sequence analysisCell-free systemLysis genesNonsense mutantsSynthetase geneUAA codonProtein geneAcid polypeptideSite mutantsTranslation productsInitiator regionSecond codonCistronNonpermissive cellsSame proteinPhage RNAAUG triplet[27] Prokaryotic ribosome binding sites
Steitz J. [27] Prokaryotic ribosome binding sites. Methods In Enzymology 1979, 60: 311-321. PMID: 379525, DOI: 10.1016/s0076-6879(79)60029-0.Peer-Reviewed Original Research
1977
Characterization of two mRNA · rRNA complexes implicated in the initiation of protein biosynthesis
Steitz J, Steege D. Characterization of two mRNA · rRNA complexes implicated in the initiation of protein biosynthesis. Journal Of Molecular Biology 1977, 114: 545-558. PMID: 335077, DOI: 10.1016/0022-2836(77)90177-2.Peer-Reviewed Original ResearchConceptsProtein biosynthesisEscherichia coli 16 S ribosomal RNAS ribosomal RNABase pair regionNuclease digestion studiesFragment complexAssignment of residuesRibosomal RNARRNA complexLambda PRBacteriophage lambdaMolecular understandingInitiation siteInitiation eventsStrong experimental supportMessenger RNABiosynthesisThermal denaturation studiesDenaturation studiesRNAPR transcriptsPR regionDigestion studiesMRNAComplexes