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Hsp70 and Hsp110 chaperones promote early steps of proteasome assembly

2022Journal article Open Access
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dc.contributor.authorA. C., Matias
dc.contributor.authorMatos, Joao
dc.contributor.authorDohmen, R. Jürgen
dc.contributor.authorRamos, Paula C.
dc.date.accessioned2023-02-27T11:02:50Z
dc.date.available2023-02-27T11:02:50Z
dc.date.issued2022
dc.description.abstractWhereas assembly of the 20S proteasome core particle (CP) in prokaryotes apparently occurs spontaneously, the efficiency of this process in eukaryotes relies on the dedicated assembly chaperones Ump1, Pba1-Pba2, and Pba3-Pba4. For mammals, it was reported that CP assembly initiates with formation of a complete alpha-ring that functions as a template for beta subunit incorporation. By contrast, we were not able to detect a ring composed only of a complete set of alpha subunits in S. cerevisiae. Instead, we found that the CP subunits alpha 1, alpha 2, and alpha 4 each form independent small complexes. Purification of such complexes containing alpha 4 revealed the presence of chaperones of the Hsp70/Ssa and Hsp110/Sse families. Consistently, certain small complexes containing alpha 1, alpha 2, and alpha 4 were not formed in strains lacking these chaperones. Deletion of the SSE1 gene in combination with deletions of PRE9 (alpha 3), PBA3, or UMP1 genes resulted in severe synthetic growth defects, high levels of ubiquitin-conjugates, and an accumulation of distinct small complexes with alpha subunits. Our study shows that Hsp70 and Hsp110 chaperones cooperate to promote the folding of individual alpha subunits and/or their assembly with other CP subunits, Ump1, and Pba1-Pba4 in subsequent steps.pt_PT
dc.description.sponsorshipPOCTI/32621/BME/2000
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.doi10.3390/biom13010011pt_PT
dc.identifier.eissn2218-273X
dc.identifier.urihttp://hdl.handle.net/10400.1/19133
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherMDPIpt_PT
dc.relationAnalysis of the early precursors in the 20S proteasome assembly pathway
dc.relationControl of eukaryotic proteasome biogenesis by chaperones
dc.relationStrategic Project - LA 23 - 2011-2012
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/pt_PT
dc.subjectProteasome biogenesispt_PT
dc.subjectChaperonespt_PT
dc.subjectHsp70pt_PT
dc.subjectHsp110pt_PT
dc.subjectSsa1pt_PT
dc.subjectSse1pt_PT
dc.titleHsp70 and Hsp110 chaperones promote early steps of proteasome assemblypt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleAnalysis of the early precursors in the 20S proteasome assembly pathway
oaire.awardTitleControl of eukaryotic proteasome biogenesis by chaperones
oaire.awardTitleStrategic Project - LA 23 - 2011-2012
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/POCI/POCI%2FBIA-PRO%2F58344%2F2004/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FQUI-BIQ%2F098427%2F2008/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/PEst-OE%2FEQB%2FLA0023%2F2011/PT
oaire.citation.issue1pt_PT
oaire.citation.startPage11pt_PT
oaire.citation.titleBiomoleculespt_PT
oaire.citation.volume13pt_PT
oaire.fundingStreamPOCI
oaire.fundingStream3599-PPCDT
oaire.fundingStream6817 - DCRRNI ID
person.familyNameMatias
person.givenNameAna Catarina
person.identifier.ciencia-id701D-019D-0779
person.identifier.orcid0000-0002-6385-9117
person.identifier.ridA-9430-2014
person.identifier.scopus-author-id55232110200
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
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relation.isAuthorOfPublication.latestForDiscovery2b71c7a8-f595-4ca3-ba39-5553c33deb3c
relation.isProjectOfPublication06cc1fa1-d1d5-4483-904c-b70f678fdcf5
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