Diiron centre mutations in Ciona intestinalis alternative oxidase abolish enzymatic activity and prevent rescue of cytochrome oxidase deficiency in flies

dc.contributor.authorAndjelkovic, Ana
dc.contributor.authorOliveira, Marcos T. [UNESP]
dc.contributor.authorCannino, Giuseppe
dc.contributor.authorYalgin, Cagri
dc.contributor.authorDhandapani, Praveen K.
dc.contributor.authorDufour, Eric
dc.contributor.authorRustin, Pierre
dc.contributor.authorSzibor, Marten
dc.contributor.authorJacobs, Howard T.
dc.contributor.institutionTampere Univ
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniv Helsinki
dc.contributor.institutionINSERM
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.date.accessioned2018-11-26T16:18:57Z
dc.date.available2018-11-26T16:18:57Z
dc.date.issued2015-12-17
dc.description.abstractThe mitochondrial alternative oxidase, AOX, carries out the non proton-motive re-oxidation of ubiquinol by oxygen in lower eukaryotes, plants and some animals. Here we created a modified version of AOX from Ciona instestinalis, carrying mutations at conserved residues predicted to be required for chelation of the diiron prosthetic group. The modified protein was stably expressed in mammalian cells or flies, but lacked enzymatic activity and was unable to rescue the phenotypes of flies knocked down for a subunit of cytochrome oxidase. The mutated AOX transgene is thus a potentially useful tool in studies of the physiological effects of AOX expression.en
dc.description.affiliationTampere Univ, BioMediTech, FI-33014 Tampere, Finland
dc.description.affiliationTampere Univ, Tampere Univ Hosp, FI-33014 Tampere, Finland
dc.description.affiliationUniv Estadual Paulista, Fac Ciencias Agr & Vet, Dept Tecnol, BR-14884900 Jaboticabal, SP, Brazil
dc.description.affiliationUniv Helsinki, Inst Biotechnol, FI-00014 Helsinki, Finland
dc.description.affiliationINSERM, UMR 1141, F-75019 Paris, France
dc.description.affiliationUniv Paris 07, Fac Med Denis Diderot, Hop Robert Debre, F-75019 Paris, France
dc.description.affiliationUnespUniv Estadual Paulista, Fac Ciencias Agr & Vet, Dept Tecnol, BR-14884900 Jaboticabal, SP, Brazil
dc.description.sponsorshipAcademy of Finland (CoE grant)
dc.description.sponsorshipEuropean Research Council
dc.description.sponsorshipEU (Marie Curie International Incoming Fellowship)
dc.description.sponsorshipTampere University Hospital Medical Research Fund
dc.description.sponsorshipSigrid Juselius Foundation
dc.description.sponsorshipIdAcademy of Finland (CoE grant): 272376
dc.description.sponsorshipIdEuropean Research Council: 232738
dc.description.sponsorshipIdEU (Marie Curie International Incoming Fellowship): 328988
dc.format.extent9
dc.identifierhttp://dx.doi.org/10.1038/srep18295
dc.identifier.citationScientific Reports. London: Nature Publishing Group, v. 5, 9 p., 2015.
dc.identifier.doi10.1038/srep18295
dc.identifier.fileWOS000366569400001.pdf
dc.identifier.issn2045-2322
dc.identifier.urihttp://hdl.handle.net/11449/161054
dc.identifier.wosWOS:000366569400001
dc.language.isoeng
dc.publisherNature Publishing Group
dc.relation.ispartofScientific Reports
dc.relation.ispartofsjr1,533
dc.rights.accessRightsAcesso aberto
dc.sourceWeb of Science
dc.titleDiiron centre mutations in Ciona intestinalis alternative oxidase abolish enzymatic activity and prevent rescue of cytochrome oxidase deficiency in fliesen
dc.typeArtigo
dcterms.rightsHolderNature Publishing Group
unesp.author.orcid0000-0001-6690-5329[6]
unesp.departmentTecnologia - FCAVpt

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