Rpn7 Is Required for the Structural Integrity of the 26 S Proteasome of Saccharomyces cerevisiae
Rpn7 Is Required for the Structural Integrity of the 26 S Proteasome of Saccharomyces cerevisiae
No Thumbnail Available
Files
There are no files associated with this item.
Date
2004
Authors
Editors
Journal ISSN
Electronic ISSN
ISBN
Bibliographical data
Publisher
Series
DOI (citable link)
International patent number
Link to the license
oops
EU project number
Project
Open Access publication
Collections
Title in another language
Publication type
Journal article
Publication status
Published
Published in
The Journal of Biological Chemistry : JBC ; 279 (2004), 26. - pp. 27168-27176. - ISSN 0021-9258. - eISSN 1083-351X
Abstract
Rpn7 is one of the lid subunits of the 26 S proteasome regulatory particle. The RPN7 gene is known to be essential, but its function remains to be elucidated. To explore the function of Rpn7, we isolated and characterized temperature-sensitive rpn7 mutants. All of the rpn7 mutants obtained accumulated poly-ubiquitinated proteins when grown at the restrictive temperature. The N-end rule substrate (Ub-Arg-beta-galactosidase), the UFD pathway substrate (Ub-Pro-beta-galactosidase), and cell cycle regulators (Pds1 and Clb2) were found to be stabilized in experiments using one of the rpn7 mutants termed rpn7-3 at the restrictive temperature, indicating its defect in the ubiquitin-proteasome pathway. Subsequent analysis of the structure of the 26 S proteasome in rpn7-3 cells suggested that the defect was in the assembly of the 26 S holoenzyme. The most striking characteristic of the proteasome of the rpn7-3 mutant was that a lid subcomplex affinity-purified from the rpn7-3 cells grown at the restrictive temperature contained only 5 of the 8 lid components, a phenomenon that has not been reported in the previously isolated lid mutants. From these results, we concluded that Rpn7 is required for the integrity of the 26 S complex by establishing a correct lid structure.
Summary in another language
Subject (DDC)
570 Biosciences, Biology
Keywords
Conference
Review
undefined / . - undefined, undefined. - (undefined; undefined)
Cite This
ISO 690
ISONO, Erika, Yasushi SAEKI, Hideyoshi YOKOSAWA, Akio TOH-E, 2004. Rpn7 Is Required for the Structural Integrity of the 26 S Proteasome of Saccharomyces cerevisiae. In: The Journal of Biological Chemistry : JBC. 279(26), pp. 27168-27176. ISSN 0021-9258. eISSN 1083-351X. Available under: doi: 10.1074/jbc.M314231200BibTex
@article{Isono2004-06-25Requi-42151, year={2004}, doi={10.1074/jbc.M314231200}, title={Rpn7 Is Required for the Structural Integrity of the 26 S Proteasome of Saccharomyces cerevisiae}, number={26}, volume={279}, issn={0021-9258}, journal={The Journal of Biological Chemistry : JBC}, pages={27168--27176}, author={Isono, Erika and Saeki, Yasushi and Yokosawa, Hideyoshi and Toh-e, Akio} }
RDF
<rdf:RDF xmlns:dcterms="http://purl.org/dc/terms/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#" xmlns:foaf="http://xmlns.com/foaf/0.1/" xmlns:void="http://rdfs.org/ns/void#" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/server/rdf/resource/123456789/42151"> <dcterms:abstract xml:lang="eng">Rpn7 is one of the lid subunits of the 26 S proteasome regulatory particle. The RPN7 gene is known to be essential, but its function remains to be elucidated. To explore the function of Rpn7, we isolated and characterized temperature-sensitive rpn7 mutants. All of the rpn7 mutants obtained accumulated poly-ubiquitinated proteins when grown at the restrictive temperature. The N-end rule substrate (Ub-Arg-beta-galactosidase), the UFD pathway substrate (Ub-Pro-beta-galactosidase), and cell cycle regulators (Pds1 and Clb2) were found to be stabilized in experiments using one of the rpn7 mutants termed rpn7-3 at the restrictive temperature, indicating its defect in the ubiquitin-proteasome pathway. Subsequent analysis of the structure of the 26 S proteasome in rpn7-3 cells suggested that the defect was in the assembly of the 26 S holoenzyme. The most striking characteristic of the proteasome of the rpn7-3 mutant was that a lid subcomplex affinity-purified from the rpn7-3 cells grown at the restrictive temperature contained only 5 of the 8 lid components, a phenomenon that has not been reported in the previously isolated lid mutants. From these results, we concluded that Rpn7 is required for the integrity of the 26 S complex by establishing a correct lid structure.</dcterms:abstract> <dcterms:title>Rpn7 Is Required for the Structural Integrity of the 26 S Proteasome of Saccharomyces cerevisiae</dcterms:title> <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/42151"/> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2018-04-24T12:46:59Z</dcterms:available> <dc:creator>Saeki, Yasushi</dc:creator> <dc:creator>Toh-e, Akio</dc:creator> <dc:language>eng</dc:language> <dc:contributor>Yokosawa, Hideyoshi</dc:contributor> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2018-04-24T12:46:59Z</dc:date> <dc:contributor>Isono, Erika</dc:contributor> <dc:contributor>Toh-e, Akio</dc:contributor> <dcterms:issued>2004-06-25</dcterms:issued> <dc:creator>Yokosawa, Hideyoshi</dc:creator> <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/> <foaf:homepage rdf:resource="http://localhost:8080/"/> <dc:creator>Isono, Erika</dc:creator> <dc:contributor>Saeki, Yasushi</dc:contributor> </rdf:Description> </rdf:RDF>
Internal note
xmlui.Submission.submit.DescribeStep.inputForms.label.kops_note_fromSubmitter
Examination date of dissertation
Method of financing
Comment on publication
Alliance license
Corresponding Authors der Uni Konstanz vorhanden
International Co-Authors
Bibliography of Konstanz
No