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http://purl.uniprot.org/citations/18278055http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18278055http://www.w3.org/2000/01/rdf-schema#comment"The proteasome is the central regulatory protease of eukaryotic cells. Heteroheptameric alpha-subunit and beta-subunit rings stack to form the 20S proteasome, which associates with a 19S regulatory particle (RP). Here we show that two yeast proteins, Pba3 and Pba4, form a previously unidentified 20S proteasome-assembly chaperone. Pba3-Pba4 interacts genetically and physically with specific proteasomal alpha subunits, and loss of Pba3-Pba4 causes both a reduction and a remodeling of cellular proteasomes. Notably, mutant cells accumulate proteasomes in which a second copy of the alpha4 subunit replaces alpha3. 20S proteasome-assembly defects also are associated with altered RP assembly; this unexpected result suggests that the 20S proteasome can function as an RP-assembly factor in vivo. Our data demonstrate that Pba3-Pba4 orchestrates formation of a specific type of proteasome, the first example of a trans-acting factor that controls assembly of alternative proteasomal complexes."xsd:string
http://purl.uniprot.org/citations/18278055http://purl.org/dc/terms/identifier"doi:10.1038/nsmb.1389"xsd:string
http://purl.uniprot.org/citations/18278055http://purl.uniprot.org/core/author"Funakoshi M."xsd:string
http://purl.uniprot.org/citations/18278055http://purl.uniprot.org/core/author"Hochstrasser M."xsd:string
http://purl.uniprot.org/citations/18278055http://purl.uniprot.org/core/author"Kusmierczyk A.R."xsd:string
http://purl.uniprot.org/citations/18278055http://purl.uniprot.org/core/author"Kunjappu M.J."xsd:string
http://purl.uniprot.org/citations/18278055http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18278055http://purl.uniprot.org/core/name"Nat Struct Mol Biol"xsd:string
http://purl.uniprot.org/citations/18278055http://purl.uniprot.org/core/pages"237-244"xsd:string
http://purl.uniprot.org/citations/18278055http://purl.uniprot.org/core/title"A multimeric assembly factor controls the formation of alternative 20S proteasomes."xsd:string
http://purl.uniprot.org/citations/18278055http://purl.uniprot.org/core/volume"15"xsd:string
http://purl.uniprot.org/citations/18278055http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18278055
http://purl.uniprot.org/citations/18278055http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18278055
http://purl.uniprot.org/uniprot/Q12245#attribution-3290FA1894F10E63DEBB5AC2246BD53Fhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/18278055
http://purl.uniprot.org/uniprot/Q07951#attribution-3290FA1894F10E63DEBB5AC2246BD53Fhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/18278055
http://purl.uniprot.org/uniprot/#_Q07951-mappedCitation-18278055http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18278055
http://purl.uniprot.org/uniprot/#_P40303-mappedCitation-18278055http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18278055
http://purl.uniprot.org/uniprot/#_Q12245-mappedCitation-18278055http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18278055
http://purl.uniprot.org/uniprot/#_P32379-mappedCitation-18278055http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18278055
http://purl.uniprot.org/uniprot/#_P23638-mappedCitation-18278055http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18278055
http://purl.uniprot.org/uniprot/P23638http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18278055
http://purl.uniprot.org/uniprot/P32379http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18278055
http://purl.uniprot.org/uniprot/P40303http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18278055
http://purl.uniprot.org/uniprot/Q12245http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18278055