http://purl.uniprot.org/citations/18927584 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/18927584 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/18927584 | http://www.w3.org/2000/01/rdf-schema#comment | "Blm10 is bound to the yeast proteasome core particle, a crucial protease of eukaryotic cells [corrected]. Two gates, at both ends of the CP, control the access of protein substrates to the catalytic cavity of the CP. Normally, substrate access is auto-inhibited by a closed gate conformation unless regulatory complexes are bound to the CP and translocate protein substrates in an ATP-dependent manner. Here, we provide evidence that Blm10 recognizes pre-activated open gate CPs, which are assumed to exist in an equilibrium with inactive closed gate CP. Consequently, single-capped Blm10-CP shows peptide hydrolysis activity. Under conditions of disturbed CP assembly, as well as in open gate mutants, pre-activated CP or constitutively active CP, respectively, prevail. Then, Blm10 sequesters disordered and open gate CP by forming double-capped Blm10(2)-CP in which peptide hydrolysis activity is repressed. We conclude that Blm10 distinguishes between gate conformations and regulates the activation of CP."xsd:string |
http://purl.uniprot.org/citations/18927584 | http://purl.org/dc/terms/identifier | "doi:10.1038/embor.2008.190"xsd:string |
http://purl.uniprot.org/citations/18927584 | http://purl.org/dc/terms/identifier | "doi:10.1038/embor.2008.190"xsd:string |
http://purl.uniprot.org/citations/18927584 | http://purl.uniprot.org/core/author | "Enenkel C."xsd:string |
http://purl.uniprot.org/citations/18927584 | http://purl.uniprot.org/core/author | "Enenkel C."xsd:string |
http://purl.uniprot.org/citations/18927584 | http://purl.uniprot.org/core/author | "Jechow K."xsd:string |
http://purl.uniprot.org/citations/18927584 | http://purl.uniprot.org/core/author | "Jechow K."xsd:string |
http://purl.uniprot.org/citations/18927584 | http://purl.uniprot.org/core/author | "Lehmann A."xsd:string |
http://purl.uniprot.org/citations/18927584 | http://purl.uniprot.org/core/author | "Lehmann A."xsd:string |
http://purl.uniprot.org/citations/18927584 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
http://purl.uniprot.org/citations/18927584 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
http://purl.uniprot.org/citations/18927584 | http://purl.uniprot.org/core/name | "EMBO Rep."xsd:string |
http://purl.uniprot.org/citations/18927584 | http://purl.uniprot.org/core/name | "EMBO Rep."xsd:string |
http://purl.uniprot.org/citations/18927584 | http://purl.uniprot.org/core/pages | "1237-1243"xsd:string |
http://purl.uniprot.org/citations/18927584 | http://purl.uniprot.org/core/pages | "1237-1243"xsd:string |
http://purl.uniprot.org/citations/18927584 | http://purl.uniprot.org/core/title | "Blm10 binds to pre-activated proteasome core particles with open gate conformation."xsd:string |
http://purl.uniprot.org/citations/18927584 | http://purl.uniprot.org/core/title | "Blm10 binds to pre-activated proteasome core particles with open gate conformation."xsd:string |
http://purl.uniprot.org/citations/18927584 | http://purl.uniprot.org/core/volume | "9"xsd:string |
http://purl.uniprot.org/citations/18927584 | http://purl.uniprot.org/core/volume | "9"xsd:string |
http://purl.uniprot.org/citations/18927584 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/18927584 |
http://purl.uniprot.org/citations/18927584 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/18927584 |
http://purl.uniprot.org/citations/18927584 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/18927584 |
http://purl.uniprot.org/citations/18927584 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/18927584 |