Structural basis for dimethylarginine recognition by the Tudor domains of human SMN and SPF30 proteins
Tripsianes K, Madl T, Machyna M, Fessas D, Englbrecht C, Fischer U, Neugebauer KM, Sattler M. Structural basis for dimethylarginine recognition by the Tudor domains of human SMN and SPF30 proteins. Nature Structural & Molecular Biology 2011, 18: 1414-1420. PMID: 22101937, DOI: 10.1038/nsmb.2185.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceArginineBinding SitesHumansModels, MolecularMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularProtein Structure, TertiaryRibonucleoproteins, Small NuclearRNA Splicing FactorsSequence AlignmentSMN Complex ProteinsSurvival of Motor Neuron 1 ProteinThermodynamicsCotranscriptional spliceosome assembly and splicing are independent of the Prp40p WW domain
Görnemann J, Barrandon C, Hujer K, Rutz B, Rigaut G, Kotovic KM, Faux C, Neugebauer KM, Séraphin B. Cotranscriptional spliceosome assembly and splicing are independent of the Prp40p WW domain. RNA 2011, 17: 2119-2129. PMID: 22020974, PMCID: PMC3222125, DOI: 10.1261/rna.02646811.Peer-Reviewed Original ResearchMeSH KeywordsGene Expression Regulation, FungalHumansProtein BindingProtein Structure, TertiaryRibonucleoprotein, U1 Small NuclearRNA PrecursorsRNA SplicingSpliceosomesTranscription, GeneticYeastsConceptsC-terminal domainWW domainsSpliceosome assemblyU1 snRNPPol II C-terminal domainCotranscriptional spliceosome assemblyComplex cellular functionsRNA polymerase IIProtein-protein interactionsPre-mRNA splicingU2 snRNP recruitmentSplice site recognitionCotranscriptional recruitmentTranscriptional machineryPolymerase IIPol IIU5 snRNPLarge subunitSplicing factorsCellular functionsStable heterodimerComplex assemblyPrp40Spliceosome formationAffinity purification