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http://purl.uniprot.org/citations/33548203http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/33548203http://www.w3.org/2000/01/rdf-schema#comment"The Integrator is a specialized 3' end-processing complex involved in cleavage and transcription termination of a subset of nascent RNA polymerase II transcripts, including small nuclear RNAs (snRNAs). We provide evidence of the modular nature of the Integrator complex by biochemically characterizing its two subcomplexes, INTS5/8 and INTS10/13/14. Using cryoelectron microscopy (cryo-EM), we determined a 3.5-Å-resolution structure of the INTS4/9/11 ternary complex, which constitutes Integrator's catalytic core. Our structure reveals the spatial organization of the catalytic nuclease INTS11, bound to its catalytically impaired homolog INTS9 via several interdependent interfaces. INTS4, a helical repeat protein, plays a key role in stabilizing nuclease domains and other components. In this assembly, all three proteins form a composite electropositive groove, suggesting a putative RNA binding path within the complex. Comparison with other 3' end-processing machineries points to distinct features and a unique architecture of the Integrator's catalytic module."xsd:string
http://purl.uniprot.org/citations/33548203http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2021.01.005"xsd:string
http://purl.uniprot.org/citations/33548203http://purl.uniprot.org/core/author"Galej W.P."xsd:string
http://purl.uniprot.org/citations/33548203http://purl.uniprot.org/core/author"Pfleiderer M.M."xsd:string
http://purl.uniprot.org/citations/33548203http://purl.uniprot.org/core/date"2021"xsd:gYear
http://purl.uniprot.org/citations/33548203http://purl.uniprot.org/core/name"Mol Cell"xsd:string
http://purl.uniprot.org/citations/33548203http://purl.uniprot.org/core/pages"1246-1259.e8"xsd:string
http://purl.uniprot.org/citations/33548203http://purl.uniprot.org/core/title"Structure of the catalytic core of the Integrator complex."xsd:string
http://purl.uniprot.org/citations/33548203http://purl.uniprot.org/core/volume"81"xsd:string
http://purl.uniprot.org/citations/33548203http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/33548203
http://purl.uniprot.org/citations/33548203http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/33548203
http://purl.uniprot.org/uniprot/Q96SY0#attribution-B69049F557CB655F97619ABFDCE33866http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/33548203
http://purl.uniprot.org/uniprot/#_Q5TA45-mappedCitation-33548203http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/33548203
http://purl.uniprot.org/uniprot/#_Q96HW7-mappedCitation-33548203http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/33548203
http://purl.uniprot.org/uniprot/#_Q9NV88-mappedCitation-33548203http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/33548203
http://purl.uniprot.org/uniprot/Q5TA45http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/33548203
http://purl.uniprot.org/uniprot/Q9NV88http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/33548203
http://purl.uniprot.org/uniprot/Q96HW7http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/33548203