2021
Structural analyses of an RNA stability element interacting with poly(A)
Torabi SF, Chen YL, Zhang K, Wang J, DeGregorio SJ, Vaidya AT, Su Z, Pabit SA, Chiu W, Pollack L, Steitz JA. Structural analyses of an RNA stability element interacting with poly(A). Proceedings Of The National Academy Of Sciences Of The United States Of America 2021, 118: e2026656118. PMID: 33785601, PMCID: PMC8040590, DOI: 10.1073/pnas.2026656118.Peer-Reviewed Original ResearchConceptsRNA stability elementCis-acting RNA elementsGlobal conformational changesRich internal loopCryo-electron microscopyRice transposable elementsDiverse genomesDouble-helical regionsSmall-angle X-ray scatteringEne motifTransposable elementsGlobal structural changesRNA interactionsRNA stabilityBioinformatics studiesRNA elementsStability elementShort helixConformational changesDecay pathwaysInternal loopBiochemical structureTriplex structureBindingMotif
2008
Conserved motifs in both CPSF73 and CPSF100 are required to assemble the active endonuclease for histone mRNA 3′‐end maturation
Kolev NG, Yario TA, Benson E, Steitz JA. Conserved motifs in both CPSF73 and CPSF100 are required to assemble the active endonuclease for histone mRNA 3′‐end maturation. EMBO Reports 2008, 9: 1013-1018. PMID: 18688255, PMCID: PMC2572124, DOI: 10.1038/embor.2008.146.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceBase SequenceCell LineCleavage And Polyadenylation Specificity FactorConserved SequenceEndonucleasesEnzyme ActivationHeLa CellsHistonesHumansMolecular Sequence DataProtein Structure, TertiaryProtein SubunitsRNA 3' End ProcessingRNA PrecursorsRNA, MessengerConceptsPre-messenger RNAPolyadenylation specificity factorMammalian proteinsRNase ZConserved motifsHistone mRNASpecificity factorEndonucleolytic cleavageActive endonucleaseEndonuclease activityMBL familyComplex machineryMessenger RNAPoint mutationsCPSF73CPSF100Process of maturationMaturation processRNAProteinMotifMRNAMaturationEukaryotesCleavage
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
2002
Exclusive Interaction of the 15.5 kD Protein with the Terminal Box C/D Motif of a Methylation Guide snoRNP
Szewczak LB, DeGregorio SJ, Strobel SA, Steitz JA. Exclusive Interaction of the 15.5 kD Protein with the Terminal Box C/D Motif of a Methylation Guide snoRNP. Cell Chemical Biology 2002, 9: 1095-1107. PMID: 12401494, DOI: 10.1016/s1074-5521(02)00239-9.Peer-Reviewed Original ResearchConceptsBox C/D motifKD proteinD motifBox C/D snoRNAsBox C/D snoRNPsSite-specific methylationSpliceosomal RNAsDeleterious substitutionsD snoRNAsD snoRNPsBox DExclusive interactionsInteraction sitesXenopus oocytesSnoRNPsProteinMotifSnoRNAsVivoMethylationA89Single interaction siteRNAExocyclic amineOocytes