2013
Assembly of the SLIP1–SLBP Complex on Histone mRNA Requires Heterodimerization and Sequential Binding of SLBP Followed by SLIP1
Bansal N, Zhang M, Bhaskar A, Itotia P, Lee E, Shlyakhtenko LS, Lam TT, Fritz A, Berezney R, Lyubchenko YL, Stafford WF, Thapar R. Assembly of the SLIP1–SLBP Complex on Histone mRNA Requires Heterodimerization and Sequential Binding of SLBP Followed by SLIP1. Biochemistry 2013, 52: 520-536. PMID: 23286197, PMCID: PMC3580866, DOI: 10.1021/bi301074r.Peer-Reviewed Original ResearchCarrier ProteinsHistonesHumansKineticsMRNA Cleavage and Polyadenylation FactorsMutagenesis, Site-DirectedMutant ProteinsNuclear ProteinsPeptide FragmentsPhosphorylationPoint MutationProtein BindingProtein Interaction Domains and MotifsProtein MultimerizationProtein Processing, Post-TranslationalRecombinant ProteinsRNA FoldingRNA, MessengerRNA-Binding ProteinsSerineThreonineTyrosine
2012
The Prolyl Isomerase Pin1 Targets Stem-Loop Binding Protein (SLBP) To Dissociate the SLBP-Histone mRNA Complex Linking Histone mRNA Decay with SLBP Ubiquitination
Krishnan N, Lam TT, Fritz A, Rempinski D, O'Loughlin K, Minderman H, Berezney R, Marzluff WF, Thapar R. The Prolyl Isomerase Pin1 Targets Stem-Loop Binding Protein (SLBP) To Dissociate the SLBP-Histone mRNA Complex Linking Histone mRNA Decay with SLBP Ubiquitination. Molecular And Cellular Biology 2012, 32: 4306-4322. PMID: 22907757, PMCID: PMC3486140, DOI: 10.1128/mcb.00382-12.Peer-Reviewed Original ResearchMeSH KeywordsCell CycleCell Line, TumorCell NucleusDown-RegulationHEK293 CellsHeLa CellsHistonesHumansMRNA Cleavage and Polyadenylation FactorsNIMA-Interacting Peptidylprolyl IsomeraseNuclear ProteinsPeptidylprolyl IsomeraseProtein Phosphatase 2RNA InterferenceRNA StabilityRNA, MessengerRNA, Small InterferingRNA-Binding ProteinsUbiquitinationConceptsStem-loop binding proteinHistone mRNADegradation of SLBPMRNA stabilityBinding proteinHistone mRNA stabilityRNA degradation machineryHistone mRNA decayS phaseProtein phosphatase 2AHistone mRNA degradationCore histone mRNAsExosome-mediated degradationDownregulation of Pin1Ubiquitin-proteasome systemMRNA 3' endsProlyl isomerase Pin1Phosphatase 2ADegradation machineryMRNA decayMRNA degradationProteasome systemIsomerase Pin1MRNA complexesUntranslated regionInteraction of the Histone mRNA Hairpin with Stem–Loop Binding Protein (SLBP) and Regulation of the SLBP–RNA Complex by Phosphorylation and Proline Isomerization
Zhang M, Lam TT, Tonelli M, Marzluff WF, Thapar R. Interaction of the Histone mRNA Hairpin with Stem–Loop Binding Protein (SLBP) and Regulation of the SLBP–RNA Complex by Phosphorylation and Proline Isomerization. Biochemistry 2012, 51: 3215-3231. PMID: 22439849, PMCID: PMC3328597, DOI: 10.1021/bi2018255.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesDrosophila ProteinsHistonesHumansKineticsMolecular Sequence DataMRNA Cleavage and Polyadenylation FactorsNuclear ProteinsNucleic Acid ConformationPhosphorylationProlineRNA, MessengerRNA-Binding ProteinsConceptsStem-loop binding proteinStem-loop structureHistone mRNAProline isomerizationThreonine phosphorylationEnd formationC base pairsReplication-dependent histone mRNAsBase pairsBinding proteinPossible structural roleAdjacent prolineHistone proteinsRibonucleoprotein complexesHelix motifMRNA hairpinsMRNA complexesUntranslated regionStructural roleFirst binding sitePhosphorylationProteinComplex dissociationCritical hingeMRNA