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PACemakers of proteasome core particle assembly

dc.contributor.authorRamos, Paula C.
dc.contributor.authorDohmen, R. Juergen
dc.date.accessioned2018-12-07T14:58:15Z
dc.date.available2018-12-07T14:58:15Z
dc.date.issued2008-09
dc.description.abstractThe 26S proteasome mediates ubiquitin-dependent proteolysis in eukaryotic cells. A number of studies including very recent ones have revealed that assembly of its 20S catalytic core particle is an ordered process that involves several conserved proteasome assembly chaperones (PACs). Two heterodimeric chaperones, PAC1-PAC2 and PAC3-PAC4, promote the assembly of rings composed of seven alpha subunits. Subsequently, P subunits join to form half-proteasome precursor complexes containing all but one of the 14 subunits. These complexes lack the beta 7 subunit but contain UMP1, another assembly chaperone, and in yeast, at least to some degree, the activator protein Blm10. Dimerization of two such complexes is triggered by incorporation of beta 7, whose C-terminal extension reaches out into the other half to stabilize the newly formed 20S particle. The process is completed by the maturation of active sites and subsequent degradation of UMP1 and PAC1-PAC2.
dc.description.sponsorshipFundacao para a Ciencia e Tecnologia; Deutsche Forschungsgemeinschaft
dc.identifier.doihttps://doi.org/10.1016/j.str.2008.07.001
dc.identifier.issn0969-2126
dc.identifier.urihttp://hdl.handle.net/10400.1/11938
dc.language.isoeng
dc.peerreviewedyes
dc.publisherCell Press
dc.subjectMammalian 20S Proteasomes
dc.subjectActive-Site Formation
dc.subjectS-Proteasome
dc.subjectEndoplasmic-Reticulum
dc.subjectAntigen Presentation
dc.subjectSubunit Composition
dc.subjectCrystal-Structure
dc.subjectYeast
dc.subjectMaturation
dc.subjectProtein
dc.titlePACemakers of proteasome core particle assembly
dc.typejournal article
dspace.entity.typePublication
oaire.citation.endPage1304
oaire.citation.issue9
oaire.citation.startPage1296
oaire.citation.titleStructure
oaire.citation.volume16
rcaap.rightsopenAccess
rcaap.typearticle

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