Role of C-terminal extensions of subunits beta 2 and beta 7 in assembly and activity of eukaryotic proteasomes
Autor(a) principal: | |
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Data de Publicação: | 2004 |
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/10400.1/11122 |
Resumo: | A close inspection of the crystal structure of the yeast 20 S proteasome revealed that a prominent connection between the two beta-rings is mediated by the subunit beta7/ Pre4. Its C-terminal extension intercalates between the beta1/Pre3 and beta2/Pup1 subunits on the opposite ring. We show that the interactions promoted by the beta7/Pre4 tail are important to facilitate the formation of 20 S particles from two half-proteasome precursor complexes and/or to stabilize mature 20 S proteasomes. The deletion of 19 residues from the beta7/Pre4 C terminus leads to an accumulation of half-proteasome precursor complexes containing the maturation factor Ump1. The C-terminal extension of beta7/Pre4, which forms several hydrogen bonds with beta1/Pre3, is in addition required for the post-acidic activity mediated by the latter subunit. Deletion of the C-terminal tail of beta7/Pre4 results in an inhibition of beta1/Pre3 propeptide processing and abrogation of post-acidic activity. Our data obtained with yeast strains that expressed the mature form of Pre3 lacking its propeptide suggest that interactions between the Pre4 C terminus and Pre3 stabilize a conformation of its active site, which is essential for post-acidic activity. Deletion of the C-terminal extension of beta2/Pup1, which wraps around beta3/Pup3 within the same beta-ring, is lethal, indicating that this extension serves an essential function in proteasome assembly or stability. |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Role of C-terminal extensions of subunits beta 2 and beta 7 in assembly and activity of eukaryotic proteasomesMammalian 20S proteasomeSaccharomyces-CerevisiaeSite formationYeastMaturationResolutionParticleAcidophilumPropeptidesCompletionA close inspection of the crystal structure of the yeast 20 S proteasome revealed that a prominent connection between the two beta-rings is mediated by the subunit beta7/ Pre4. Its C-terminal extension intercalates between the beta1/Pre3 and beta2/Pup1 subunits on the opposite ring. We show that the interactions promoted by the beta7/Pre4 tail are important to facilitate the formation of 20 S particles from two half-proteasome precursor complexes and/or to stabilize mature 20 S proteasomes. The deletion of 19 residues from the beta7/Pre4 C terminus leads to an accumulation of half-proteasome precursor complexes containing the maturation factor Ump1. The C-terminal extension of beta7/Pre4, which forms several hydrogen bonds with beta1/Pre3, is in addition required for the post-acidic activity mediated by the latter subunit. Deletion of the C-terminal tail of beta7/Pre4 results in an inhibition of beta1/Pre3 propeptide processing and abrogation of post-acidic activity. Our data obtained with yeast strains that expressed the mature form of Pre3 lacking its propeptide suggest that interactions between the Pre4 C terminus and Pre3 stabilize a conformation of its active site, which is essential for post-acidic activity. Deletion of the C-terminal extension of beta2/Pup1, which wraps around beta3/Pup3 within the same beta-ring, is lethal, indicating that this extension serves an essential function in proteasome assembly or stability.AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INCSapientiaRamos, Paula CMarques, AJLondon, MKDohmen, RJ2018-12-07T14:52:34Z2004-042004-04-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.1/11122eng0021-925810.1074/jbc.M308757200info: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:RCAAP2023-07-24T10:22:52Zoai:sapientia.ualg.pt:10400.1/11122Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T20:02:38.756193Repositório 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 |
Role of C-terminal extensions of subunits beta 2 and beta 7 in assembly and activity of eukaryotic proteasomes |
title |
Role of C-terminal extensions of subunits beta 2 and beta 7 in assembly and activity of eukaryotic proteasomes |
spellingShingle |
Role of C-terminal extensions of subunits beta 2 and beta 7 in assembly and activity of eukaryotic proteasomes Ramos, Paula C Mammalian 20S proteasome Saccharomyces-Cerevisiae Site formation Yeast Maturation Resolution Particle Acidophilum Propeptides Completion |
title_short |
Role of C-terminal extensions of subunits beta 2 and beta 7 in assembly and activity of eukaryotic proteasomes |
title_full |
Role of C-terminal extensions of subunits beta 2 and beta 7 in assembly and activity of eukaryotic proteasomes |
title_fullStr |
Role of C-terminal extensions of subunits beta 2 and beta 7 in assembly and activity of eukaryotic proteasomes |
title_full_unstemmed |
Role of C-terminal extensions of subunits beta 2 and beta 7 in assembly and activity of eukaryotic proteasomes |
title_sort |
Role of C-terminal extensions of subunits beta 2 and beta 7 in assembly and activity of eukaryotic proteasomes |
author |
Ramos, Paula C |
author_facet |
Ramos, Paula C Marques, AJ London, MK Dohmen, RJ |
author_role |
author |
author2 |
Marques, AJ London, MK Dohmen, RJ |
author2_role |
author author author |
dc.contributor.none.fl_str_mv |
Sapientia |
dc.contributor.author.fl_str_mv |
Ramos, Paula C Marques, AJ London, MK Dohmen, RJ |
dc.subject.por.fl_str_mv |
Mammalian 20S proteasome Saccharomyces-Cerevisiae Site formation Yeast Maturation Resolution Particle Acidophilum Propeptides Completion |
topic |
Mammalian 20S proteasome Saccharomyces-Cerevisiae Site formation Yeast Maturation Resolution Particle Acidophilum Propeptides Completion |
description |
A close inspection of the crystal structure of the yeast 20 S proteasome revealed that a prominent connection between the two beta-rings is mediated by the subunit beta7/ Pre4. Its C-terminal extension intercalates between the beta1/Pre3 and beta2/Pup1 subunits on the opposite ring. We show that the interactions promoted by the beta7/Pre4 tail are important to facilitate the formation of 20 S particles from two half-proteasome precursor complexes and/or to stabilize mature 20 S proteasomes. The deletion of 19 residues from the beta7/Pre4 C terminus leads to an accumulation of half-proteasome precursor complexes containing the maturation factor Ump1. The C-terminal extension of beta7/Pre4, which forms several hydrogen bonds with beta1/Pre3, is in addition required for the post-acidic activity mediated by the latter subunit. Deletion of the C-terminal tail of beta7/Pre4 results in an inhibition of beta1/Pre3 propeptide processing and abrogation of post-acidic activity. Our data obtained with yeast strains that expressed the mature form of Pre3 lacking its propeptide suggest that interactions between the Pre4 C terminus and Pre3 stabilize a conformation of its active site, which is essential for post-acidic activity. Deletion of the C-terminal extension of beta2/Pup1, which wraps around beta3/Pup3 within the same beta-ring, is lethal, indicating that this extension serves an essential function in proteasome assembly or stability. |
publishDate |
2004 |
dc.date.none.fl_str_mv |
2004-04 2004-04-01T00:00:00Z 2018-12-07T14:52:34Z |
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/10400.1/11122 |
url |
http://hdl.handle.net/10400.1/11122 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
0021-9258 10.1074/jbc.M308757200 |
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 |
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC |
publisher.none.fl_str_mv |
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC |
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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1799133260829163520 |