2012
Tri-snRNP-associated proteins interact with subunits of the TRAMP and nuclear exosome complexes, linking RNA decay and pre-mRNA splicing
Nag A, Steitz JA. Tri-snRNP-associated proteins interact with subunits of the TRAMP and nuclear exosome complexes, linking RNA decay and pre-mRNA splicing. RNA Biology 2012, 9: 334-342. PMID: 22336707, PMCID: PMC3384585, DOI: 10.4161/rna.19431.Peer-Reviewed Original ResearchConceptsDecay machineryMRNA splicingRNA decay machineryRNA decay factorsTri-snRNP complexNuclear exosome complexPM/SclYeast counterpartIntergenic transcriptsSnoRNA biogenesisExosome complexTri-snRNPRNA decayRRNA processingPhosphorylation sitesMRNA processingPutative componentsMtr4Prp31MachinerySplicingDifferent pathwaysProteinSpliceosomeBiogenesis
2003
Splicing-Dependent and -Independent Modes of Assembly for Intron-Encoded Box C/D snoRNPs in Mammalian Cells
Hirose T, Shu MD, Steitz JA. Splicing-Dependent and -Independent Modes of Assembly for Intron-Encoded Box C/D snoRNPs in Mammalian Cells. Molecular Cell 2003, 12: 113-123. PMID: 12887897, DOI: 10.1016/s1097-2765(03)00267-3.Peer-Reviewed Original ResearchConceptsBox C/D snoRNAsSplice siteSnoRNP proteinsD snoRNAsSnoRNP assemblyMammalian cellsHost intronBox C/D snoRNPsSmall nucleolar RNAsD snoRNPsRRNA modificationNucleolar RNAsHost genesActive splicingNts upstreamIntronsEfficient expressionSnoRNAsStable stemSplicingVivo analysisProteinAssemblyBlockage experimentsStem
2002
Site‐specific cross‐linking analyses reveal an asymmetric protein distribution for a box C/D snoRNP
Cahill NM, Friend K, Speckmann W, Li Z, Terns RM, Terns MP, Steitz JA. Site‐specific cross‐linking analyses reveal an asymmetric protein distribution for a box C/D snoRNP. The EMBO Journal 2002, 21: 3816-3828. PMID: 12110593, PMCID: PMC126121, DOI: 10.1093/emboj/cdf376.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceChromosomal Proteins, Non-HistoneMethylationMutagenesis, Site-DirectedNuclear ProteinsOligodeoxyribonucleotidesRibonucleoproteins, Small NucleolarRNA-Binding ProteinsXenopusXenopus ProteinsConceptsBox C/D snoRNPsD snoRNPsC-boxBox C/D classSite-specific cross-linking analysisBox C/D small nucleolar ribonucleoproteinsBox C/DAsymmetric protein distributionSmall nucleolar ribonucleoproteinSmall nucleolar RNAsXenopus oocyte nucleusCross-linking analysisNucleolar RNAsNucleolar ribonucleoproteinD motifBox DMutational analysisOocyte nucleusGuide sequenceWidespread modificationProtein distributionFibrillarinFunctional rescueCore proteinSnoRNPs
1998
Modification of U6 Spliceosomal RNA Is Guided by Other Small RNAs
Tycowski K, You Z, Graham P, Steitz J. Modification of U6 Spliceosomal RNA Is Guided by Other Small RNAs. Molecular Cell 1998, 2: 629-638. PMID: 9844635, DOI: 10.1016/s1097-2765(00)80161-6.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceCell FractionationCell LineCell NucleolusChromosomal Proteins, Non-HistoneDimerizationHeLa CellsHumansMethylationMiceMolecular Sequence DataNucleic Acid ConformationOligodeoxyribonucleotides, AntisenseOocytesPrecipitin TestsRibonuclease HRNA, Ribosomal, 28SRNA, Small NuclearSpliceosomesXenopus laevis
1994
Sequence and structural elements critical for U8 snRNP function in Xenopus oocytes are evolutionarily conserved.
Peculis BA, Steitz JA. Sequence and structural elements critical for U8 snRNP function in Xenopus oocytes are evolutionarily conserved. Genes & Development 1994, 8: 2241-2255. PMID: 7958892, DOI: 10.1101/gad.8.18.2241.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceBiological EvolutionChromosomal Proteins, Non-HistoneConserved SequenceFemaleMethylationMolecular Sequence DataMutagenesis, Site-DirectedMutationNucleic Acid ConformationOocytesRibonucleoproteins, Small NuclearRNA CapsRNA PrecursorsRNA Processing, Post-TranscriptionalRNA, Small NuclearXenopus
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