PACemakers of proteasome core particle assembly
Autor(a) principal: | |
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Data de Publicação: | 2008 |
Outros Autores: | |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10400.1/11938 |
Resumo: | The 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. |
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PACemakers of proteasome core particle assemblyMammalian 20S ProteasomesActive-Site FormationS-ProteasomeEndoplasmic-ReticulumAntigen PresentationSubunit CompositionCrystal-StructureYeastMaturationProteinThe 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.Fundacao para a Ciencia e Tecnologia; Deutsche ForschungsgemeinschaftCell PressSapientiaRamos, Paula C.Dohmen, R. Juergen2018-12-07T14:58:15Z2008-092008-09-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.1/11938eng0969-2126https://doi.org/10.1016/j.str.2008.07.001info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-07-24T10:23:50Zoai:sapientia.ualg.pt:10400.1/11938Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T20:03:22.352667Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
PACemakers of proteasome core particle assembly |
title |
PACemakers of proteasome core particle assembly |
spellingShingle |
PACemakers of proteasome core particle assembly Ramos, Paula C. Mammalian 20S Proteasomes Active-Site Formation S-Proteasome Endoplasmic-Reticulum Antigen Presentation Subunit Composition Crystal-Structure Yeast Maturation Protein |
title_short |
PACemakers of proteasome core particle assembly |
title_full |
PACemakers of proteasome core particle assembly |
title_fullStr |
PACemakers of proteasome core particle assembly |
title_full_unstemmed |
PACemakers of proteasome core particle assembly |
title_sort |
PACemakers of proteasome core particle assembly |
author |
Ramos, Paula C. |
author_facet |
Ramos, Paula C. Dohmen, R. Juergen |
author_role |
author |
author2 |
Dohmen, R. Juergen |
author2_role |
author |
dc.contributor.none.fl_str_mv |
Sapientia |
dc.contributor.author.fl_str_mv |
Ramos, Paula C. Dohmen, R. Juergen |
dc.subject.por.fl_str_mv |
Mammalian 20S Proteasomes Active-Site Formation S-Proteasome Endoplasmic-Reticulum Antigen Presentation Subunit Composition Crystal-Structure Yeast Maturation Protein |
topic |
Mammalian 20S Proteasomes Active-Site Formation S-Proteasome Endoplasmic-Reticulum Antigen Presentation Subunit Composition Crystal-Structure Yeast Maturation Protein |
description |
The 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. |
publishDate |
2008 |
dc.date.none.fl_str_mv |
2008-09 2008-09-01T00:00:00Z 2018-12-07T14:58:15Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10400.1/11938 |
url |
http://hdl.handle.net/10400.1/11938 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
0969-2126 https://doi.org/10.1016/j.str.2008.07.001 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.publisher.none.fl_str_mv |
Cell Press |
publisher.none.fl_str_mv |
Cell Press |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
instname_str |
Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
instacron_str |
RCAAP |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository.name.fl_str_mv |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
repository.mail.fl_str_mv |
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1799133267987791872 |