Please use this identifier to cite or link to this item: https://hdl.handle.net/10216/117909
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dc.creatorFreitas, M
dc.creatorFrancisco, T
dc.creatorRodrigues, TA
dc.creatorLismont, C
dc.creatorDomingues, P
dc.creatorPinto, MP
dc.creatorGrou, CP
dc.creatorFransen, M
dc.creatorAzevedo, JE
dc.date.accessioned2018-12-20T10:07:29Z-
dc.date.available2018-12-20T10:07:29Z-
dc.date.issued2015
dc.identifier.issn2046-2441
dc.identifier.urihttps://repositorio-aberto.up.pt/handle/10216/117909-
dc.description.abstractPeroxisomal matrix proteins are synthesized on cytosolic ribosomes and transported by the shuttling receptor PEX5 to the peroxisomal membrane docking/translocation machinery, where they are translocated into the organelle matrix. Under certain experimental conditions this protein import machinery has the remarkable capacity to accept already oligomerized proteins, a property that has heavily influenced current models on the mechanism of peroxisomal protein import. However, whether or not oligomeric proteins are really the best and most frequent clients of this machinery remain unclear. In this work, we present three lines of evidence suggesting that the peroxisomal import machinery displays a preference for monomeric proteins. First, in agreement with previous findings on catalase, we show that PEX5 binds newly synthesized (monomeric) acyl-CoA oxidase 1 (ACOX1) and urate oxidase (UOX), potently inhibiting their oligomerization. Second, in vitro import experiments suggest that monomeric ACOX1 and UOX are better peroxisomal import substrates than the corresponding oligomeric forms. Finally, we provide data strongly suggesting that although ACOX1 lacking a peroxisomal targeting signal can be imported into peroxisomes when co-expressed with ACOX1 containing its targeting signal, this import pathway is inefficient.
dc.description.sponsorshipThis work was funded by Fundo Europeu de Desenvolvimento Regional (FEDER) through the Operational Competitiveness Programme (COMPETE); by National Funds through Fundação para a Ciência e a Tecnologia (FCT) under the project FCOMP-01–0124-FEDER-022718 (PEst-C/SAU/LA0002/2011) and FCOMP-01–0124-FEDER-019731 (PTDC/BIABCM/118577/2010); by Portuguese National Mass Spectrometry Network (RNEM) through the project REDE/1504/REM/2005; and by Química Orgânica, Produtos Naturais e Agroalimentares (QOPNA) research unit funds provided by FCT, European Union, QREN, FEDER and COMPETE under the projects PEst-C/QUI/UI0062/2013 and FCOMP-01–0124-FEDER-037296. M.O.F., T.F., T.A.R., M.P.P. and C.P.G. were supported by FCT, Programa Operacional Potencial Humano (POPH) do Quadro de Referência Estratégico Nacional (QREN) and Fundo Social Europeu. The work done in Leuven was supported by grants from the ‘Fonds voor Wetenschappelijk Onderzoek-Vlaanderen (Onderzoeksproject G.0754.09)’ and the KU Leuven (OT/14/100).
dc.language.isoeng
dc.publisherThe Royal Society
dc.relationinfo:eurepo/grantAgreement/FCT/COMPETE/118577/PT
dc.relationinfo:eurepo/grantAgreement/FCT/COMPETE/132997/PT
dc.relation.ispartofOpen Biology, vol.5(4): 140236
dc.rightsopenAccess
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.subject.meshAcyl-CoA Oxidase/chemistry
dc.subject.meshAcyl-CoA Oxidase/genetics
dc.subject.meshAcyl-CoA Oxidase/metabolism
dc.subject.meshAnimals
dc.subject.meshBlotting, Western
dc.subject.meshCOS Cells
dc.subject.meshCercopithecus aethiops
dc.subject.meshCytosol/metabolism
dc.subject.meshHumans
dc.subject.meshMice
dc.subject.meshMicroscopy, Fluorescence
dc.subject.meshModels, Biological
dc.subject.meshMutation
dc.subject.meshPeroxisome-Targeting Signal 1 Receptor
dc.subject.meshPeroxisomes/metabolism
dc.subject.meshProtein Binding
dc.subject.meshProtein Multimerization
dc.subject.meshProtein Transport
dc.subject.meshRats
dc.subject.meshReceptors, Cytoplasmic and Nuclear/genetics
dc.subject.meshReceptors, Cytoplasmic and Nuclear/metabolism
dc.subject.meshSignal Transduction
dc.subject.meshUrate Oxidase/chemistry
dc.subject.meshUrate Oxidase/genetics
dc.subject.meshUrate Oxidase/metabolism
dc.titleThe peroxisomal protein import machinery displays a preference for monomeric substrates
dc.typeArtigo em Revista Científica Internacional
dc.contributor.uportoInstituto de Investigação e Inovação em Saúde
dc.identifier.doi10.1098/rsob.140236
dc.relation.publisherversionhttp://rsob.royalsocietypublishing.org/content/5/4/140236.long
Appears in Collections:I3S - Artigo em Revista Científica Internacional

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