2015
Reconstitution of the human U snRNP assembly machinery reveals stepwise Sm protein organization
Neuenkirchen N, Englbrecht C, Ohmer J, Ziegenhals T, Chari A, Fischer U. Reconstitution of the human U snRNP assembly machinery reveals stepwise Sm protein organization. The EMBO Journal 2015, 34: 1925-1941. PMID: 26069323, PMCID: PMC4547896, DOI: 10.15252/embj.201490350.Peer-Reviewed Original ResearchConceptsSMN complexAssembly machinerySm proteinsSpliceosomal U snRNPsDetailed molecular dissectionTrans-acting factorsSpontaneous conformational changesBiochemical reconstitutionPRMT5 complexU snRNPsProtein complexesMolecular dissectionProtein substratesProtein organizationIndividual proteinsConformational changesFaithful deliveryMode of actionRecombinant sourcesCoordinated actionBrownian machineMechanistic insightsSnRNPsProteinAssembly reaction
2008
An Assembly Chaperone Collaborates with the SMN Complex to Generate Spliceosomal SnRNPs
Chari A, Golas MM, Klingenhäger M, Neuenkirchen N, Sander B, Englbrecht C, Sickmann A, Stark H, Fischer U. An Assembly Chaperone Collaborates with the SMN Complex to Generate Spliceosomal SnRNPs. Cell 2008, 135: 497-509. PMID: 18984161, DOI: 10.1016/j.cell.2008.09.020.Peer-Reviewed Original ResearchConceptsSpliceosomal small nuclear ribonucleoproteinsSMN complexSm proteinsProtein unitsCore domainMRNA processing machinerySmall nuclear ribonucleoproteinSnRNP formationAssembly chaperonesPRMT5 complexClamp loaderNuclear ribonucleoproteinProcessing machinerySnRNAMode of actionPIClnStructural studiesProteinComplexesEssential componentPRMT5ChaperonesSnRNPRibonucleoproteinMachinery