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http://purl.uniprot.org/citations/28416111http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28416111http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28416111http://www.w3.org/2000/01/rdf-schema#comment"Ribosome assembly is a complex process that requires hundreds of essential assembly factors, including Rix7 (NVL2 in mammals) and Nsa1 (WDR74 in mammals). Rix7 is a type II double ring, AAA-ATPase, which is closely related to the well-known Cdc48/p97. Previous studies in Saccharomyces cerevisiae suggest that Rix7 mediates the release of Nsa1 from nucleolar pre-60S particles; however, the underlying mechanisms of this release are unknown. Through multiple structural analyses we show that S. cerevisiae Nsa1 is composed of an N-terminal seven-bladed WD40 domain followed by a lysine-rich C terminus that extends away from the WD40 domain and is required for nucleolar localization. Co-immunoprecipitation assays with the mammalian homologs identified a well-conserved interface within WDR74 that is important for its association with NVL2. We further show that WDR74 associates with the D1 AAA domain of NVL2, which represents a novel mode of binding of a substrate with a type II AAA-ATPase."xsd:string
http://purl.uniprot.org/citations/28416111http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2017.03.008"xsd:string
http://purl.uniprot.org/citations/28416111http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2017.03.008"xsd:string
http://purl.uniprot.org/citations/28416111http://purl.uniprot.org/core/author"Pillon M.C."xsd:string
http://purl.uniprot.org/citations/28416111http://purl.uniprot.org/core/author"Pillon M.C."xsd:string
http://purl.uniprot.org/citations/28416111http://purl.uniprot.org/core/author"Sobhany M."xsd:string
http://purl.uniprot.org/citations/28416111http://purl.uniprot.org/core/author"Sobhany M."xsd:string
http://purl.uniprot.org/citations/28416111http://purl.uniprot.org/core/author"Stanley R.E."xsd:string
http://purl.uniprot.org/citations/28416111http://purl.uniprot.org/core/author"Stanley R.E."xsd:string
http://purl.uniprot.org/citations/28416111http://purl.uniprot.org/core/author"Lo Y.H."xsd:string
http://purl.uniprot.org/citations/28416111http://purl.uniprot.org/core/author"Lo Y.H."xsd:string
http://purl.uniprot.org/citations/28416111http://purl.uniprot.org/core/author"Romes E.M."xsd:string
http://purl.uniprot.org/citations/28416111http://purl.uniprot.org/core/author"Romes E.M."xsd:string
http://purl.uniprot.org/citations/28416111http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/28416111http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/28416111http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/28416111http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/28416111http://purl.uniprot.org/core/pages"762-772"xsd:string
http://purl.uniprot.org/citations/28416111http://purl.uniprot.org/core/pages"762-772"xsd:string
http://purl.uniprot.org/citations/28416111http://purl.uniprot.org/core/title"Structural Analysis Reveals Features of Ribosome Assembly Factor Nsa1/WDR74 Important for Localization and Interaction with Rix7/NVL2."xsd:string
http://purl.uniprot.org/citations/28416111http://purl.uniprot.org/core/title"Structural Analysis Reveals Features of Ribosome Assembly Factor Nsa1/WDR74 Important for Localization and Interaction with Rix7/NVL2."xsd:string
http://purl.uniprot.org/citations/28416111http://purl.uniprot.org/core/volume"25"xsd:string
http://purl.uniprot.org/citations/28416111http://purl.uniprot.org/core/volume"25"xsd:string