2004
Guide RNAs with 5′ Caps and Novel Box C/D snoRNA-like Domains for Modification of snRNAs in Metazoa
Tycowski KT, Aab A, Steitz JA. Guide RNAs with 5′ Caps and Novel Box C/D snoRNA-like Domains for Modification of snRNAs in Metazoa. Current Biology 2004, 14: 1985-1995. PMID: 15556860, DOI: 10.1016/j.cub.2004.11.003.Peer-Reviewed Original ResearchConceptsModification guide RNAsGuide RNABox C/D snoRNAsInvariant G residueKink-turn structureGuide RNA genesShort guide RNASmall ribonucleoprotein particlesMetazoan organismsAncestral metazoanGuanosine capMetazoan cellsSingle intronD snoRNAsRNA genesSpliceosomal snRNAsTelomerase RNARibosomal RNASuch RNAsRibonucleoprotein particleMetazoansUpstream promoterIntronsG residuesCommon modification
2001
Dynamic Exchanges of RNA Interactions Leading to Catalytic Core Formation in the U12-Dependent Spliceosome
Frilander M, Steitz J. Dynamic Exchanges of RNA Interactions Leading to Catalytic Core Formation in the U12-Dependent Spliceosome. Molecular Cell 2001, 7: 217-226. PMID: 11172726, DOI: 10.1016/s1097-2765(01)00169-1.Peer-Reviewed Original Research
1999
Initial recognition of U12-dependent introns requires both U11/5′ splice-site and U12/branchpoint interactions
Frilander M, Steitz J. Initial recognition of U12-dependent introns requires both U11/5′ splice-site and U12/branchpoint interactions. Genes & Development 1999, 13: 851-863. PMID: 10197985, PMCID: PMC316595, DOI: 10.1101/gad.13.7.851.Peer-Reviewed Original ResearchAdenoviridaeBlotting, NorthernDose-Response Relationship, DrugEvolution, MolecularFicusinHeLa CellsHeterogeneous-Nuclear RibonucleoproteinsHumansIntronsModels, GeneticOligonucleotidesRibonuclease HRibonucleoprotein, U4-U6 Small NuclearRibonucleoproteinsRibonucleoproteins, Small NuclearRNA SplicingTime Factors
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 Research
1989
Each of the conserved sequence elements flanking the cleavage site of mammalian histone pre-mRNAs has a distinct role in the 3'-end processing reaction.
Mowry KL, Oh R, Steitz JA. Each of the conserved sequence elements flanking the cleavage site of mammalian histone pre-mRNAs has a distinct role in the 3'-end processing reaction. Molecular And Cellular Biology 1989, 9: 3105-3108. PMID: 2779556, PMCID: PMC362782, DOI: 10.1128/mcb.9.7.3105.Peer-Reviewed Original Research
1975
The 3′ terminal oligonucleotide of E.coli 16S ribosomal RNA: the sequence in both wild-type and RNase III cells is complementary to the polypurine tracts common to mRNA initiator regions
Sprague K, Steitz J. The 3′ terminal oligonucleotide of E.coli 16S ribosomal RNA: the sequence in both wild-type and RNase III cells is complementary to the polypurine tracts common to mRNA initiator regions. Nucleic Acids Research 1975, 2: 787-798. PMID: 167351, PMCID: PMC343466, DOI: 10.1093/nar/2.6.787.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceCarbodiimidesEscherichia coliOligonucleotidesPhosphoric Diester HydrolasesRibonucleasesRNA, BacterialRNA, Ribosomal
1974
Nucleotide sequences of the 5′ and 3′ termini of bacteriophage T7 early messenger RNAs synthesized in vivo: Evidence for sequence specificity in RNA processing
Kramer R, Rosenberg M, Steitz J. Nucleotide sequences of the 5′ and 3′ termini of bacteriophage T7 early messenger RNAs synthesized in vivo: Evidence for sequence specificity in RNA processing. Journal Of Molecular Biology 1974, 89: 767-776. PMID: 4449132, DOI: 10.1016/0022-2836(74)90051-5.Peer-Reviewed Original ResearchConceptsEarly regionMessenger RNAAdenylic acid residuesEarly messenger RNATwo-dimensional electrophoretic techniquesLarger precursor moleculeMonocistronic messengerRNA processingGene 0.3RNA speciesNucleotide sequenceSequence specificityAcid residuesMessenger speciesSequence analysisInitiator RNASequence heterogeneityRNAEarly RNATerminusSpecific recognition of the isolated R17 replicase initiator region by R17 coat protein
STEITZ J. Specific recognition of the isolated R17 replicase initiator region by R17 coat protein. Nature 1974, 248: 223-225. PMID: 4819415, DOI: 10.1038/248223a0.Peer-Reviewed Original ResearchHigh 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
1973
Discriminatory Ribosome Rebinding of Isolated Regions of Protein Synthesis Initiation from the Ribonucleic Acid of Bacteriophage R17
Steitz J. Discriminatory Ribosome Rebinding of Isolated Regions of Protein Synthesis Initiation from the Ribonucleic Acid of Bacteriophage R17. Proceedings Of The National Academy Of Sciences Of The United States Of America 1973, 70: 2605-2609. PMID: 4582190, PMCID: PMC427065, DOI: 10.1073/pnas.70.9.2605.Peer-Reviewed Original ResearchConceptsR17 RNARibosome-binding siteProtein synthesis initiationEscherichia coli ribosomesPolypeptide chain initiationCoat protein regionRibosome bindingBacterial ribosomeRNA moleculesInitiator regionRibosome protectionSynthesis initiationMRNA moleculesInitiator codonColi ribosomesRibosomesNative RNABacteriophage R17Bacillus stearothermophilusRNAMessenger RNARibonucleic acidR17Replicase regionFragments