2020
The gammaherpesviral TATA-box-binding protein directly interacts with the CTD of host RNA Pol II to direct late gene transcription
Castañeda A, Didychuk A, Louder R, McCollum C, Davis Z, Nogales E, Glaunsinger B. The gammaherpesviral TATA-box-binding protein directly interacts with the CTD of host RNA Pol II to direct late gene transcription. PLOS Pathogens 2020, 16: e1008843. PMID: 32886723, PMCID: PMC7498053, DOI: 10.1371/journal.ppat.1008843.Peer-Reviewed Original ResearchConceptsTATA box-binding proteinRNA polymerase IIN-terminal domainPol IIPolymerase IICellular TATA box binding proteinHost RNA polymerase IIRecruitment of RNA polymerase IIGene transcriptionLate gene transcriptionPol II recruitmentProtein interaction studiesProtein-protein contactsC-terminal domainEukaryotic transcriptionPolymerase recruitmentHuman cytomegalovirusPreinitiation complexHost transcriptionRNA PolLate genesMicroscopy-based imagingKaposi's sarcoma-associated virusTranscriptional activityPromoter recognition
2017
Usb1 controls U6 snRNP assembly through evolutionarily divergent cyclic phosphodiesterase activities
Didychuk A, Montemayor E, Carrocci T, DeLaitsch A, Lucarelli S, Westler W, Brow D, Hoskins A, Butcher S. Usb1 controls U6 snRNP assembly through evolutionarily divergent cyclic phosphodiesterase activities. Nature Communications 2017, 8: 497. PMID: 28887445, PMCID: PMC5591277, DOI: 10.1038/s41467-017-00484-w.Peer-Reviewed Original ResearchMeSH KeywordsCatalytic DomainCrystallography, X-RayEvolution, MolecularGenetic VariationHumansModels, MolecularPhosphoric Diester HydrolasesProtein BindingProtein DomainsRibonucleoprotein, U4-U6 Small NuclearRNA, Small NuclearSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSubstrate SpecificityConceptsU6 snRNP assemblySmall nuclear ribonucleoproteinSnRNP assemblyCognate RNA-binding proteinsTerminal 3'-phosphateU6 small nuclear ribonucleoproteinsRNA-binding proteinsAnti-cooperative interactionsCyclic phosphodiesterase activitySpliceosome assemblyU6 RNAHuman orthologNuclear ribonucleoproteinUSB1SpliceosomeYeastProteinPhosphodiesterase activityAntagonist proteinComplex seriesAssemblyPrp24LHP1OrthologsSnRNA
2015
Structural requirements for protein-catalyzed annealing of U4 and U6 RNAs during di-snRNP assembly
Didychuk A, Montemayor E, Brow D, Butcher S. Structural requirements for protein-catalyzed annealing of U4 and U6 RNAs during di-snRNP assembly. Nucleic Acids Research 2015, 44: 1398-1410. PMID: 26673715, PMCID: PMC4756825, DOI: 10.1093/nar/gkv1374.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceBinding, CompetitiveKineticsModels, MolecularMolecular Sequence DataMutationNucleic Acid ConformationProtein BindingProtein Structure, TertiaryRibonucleoprotein, U4-U6 Small NuclearRibonucleoproteins, Small NuclearRNA, FungalRNA, Small NuclearSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsConceptsU6 RNADi-snRNPRemodeling of RNA structureAnnealing in vitroTri-snRNP complexLarge-scale remodelingStable ternary complexRNA bindingRNA structureRibonucleoprotein complexU6 snRNPU6 snRNABase pairsPrp24RNATernary complexU4/U6Electropositive characterRate enhancementAssemblyStructural requirementsSnRNASnRNPLsm2Annealing rate