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

Detalhes bibliográficos
Autor(a) principal: Andjelkovic, Ana
Data de Publicação: 2015
Outros Autores: Oliveira, Marcos T. [UNESP], Cannino, Giuseppe, Yalgin, Cagri, Dhandapani, Praveen K., Dufour, Eric, Rustin, Pierre, Szibor, Marten, Jacobs, Howard T.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1038/srep18295
http://hdl.handle.net/11449/161054
Resumo: The 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.
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spelling Diiron centre mutations in Ciona intestinalis alternative oxidase abolish enzymatic activity and prevent rescue of cytochrome oxidase deficiency in fliesThe 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.Academy of Finland (CoE grant)European Research CouncilEU (Marie Curie International Incoming Fellowship)Tampere University Hospital Medical Research FundSigrid Juselius FoundationTampere Univ, BioMediTech, FI-33014 Tampere, FinlandTampere Univ, Tampere Univ Hosp, FI-33014 Tampere, FinlandUniv Estadual Paulista, Fac Ciencias Agr & Vet, Dept Tecnol, BR-14884900 Jaboticabal, SP, BrazilUniv Helsinki, Inst Biotechnol, FI-00014 Helsinki, FinlandINSERM, UMR 1141, F-75019 Paris, FranceUniv Paris 07, Fac Med Denis Diderot, Hop Robert Debre, F-75019 Paris, FranceUniv Estadual Paulista, Fac Ciencias Agr & Vet, Dept Tecnol, BR-14884900 Jaboticabal, SP, BrazilAcademy of Finland (CoE grant): 272376European Research Council: 232738EU (Marie Curie International Incoming Fellowship): 328988Nature Publishing GroupTampere UnivUniversidade Estadual Paulista (Unesp)Univ HelsinkiINSERMUniversidade de São Paulo (USP)Andjelkovic, AnaOliveira, Marcos T. [UNESP]Cannino, GiuseppeYalgin, CagriDhandapani, Praveen K.Dufour, EricRustin, PierreSzibor, MartenJacobs, Howard T.2018-11-26T16:18:57Z2018-11-26T16:18:57Z2015-12-17info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article9application/pdfhttp://dx.doi.org/10.1038/srep18295Scientific Reports. London: Nature Publishing Group, v. 5, 9 p., 2015.2045-2322http://hdl.handle.net/11449/16105410.1038/srep18295WOS:000366569400001WOS000366569400001.pdfWeb of Sciencereponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengScientific Reports1,533info:eu-repo/semantics/openAccess2024-06-07T15:31:17Zoai:repositorio.unesp.br:11449/161054Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T14:26:08.965514Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Diiron centre mutations in Ciona intestinalis alternative oxidase abolish enzymatic activity and prevent rescue of cytochrome oxidase deficiency in flies
title Diiron centre mutations in Ciona intestinalis alternative oxidase abolish enzymatic activity and prevent rescue of cytochrome oxidase deficiency in flies
spellingShingle Diiron centre mutations in Ciona intestinalis alternative oxidase abolish enzymatic activity and prevent rescue of cytochrome oxidase deficiency in flies
Andjelkovic, Ana
title_short Diiron centre mutations in Ciona intestinalis alternative oxidase abolish enzymatic activity and prevent rescue of cytochrome oxidase deficiency in flies
title_full Diiron centre mutations in Ciona intestinalis alternative oxidase abolish enzymatic activity and prevent rescue of cytochrome oxidase deficiency in flies
title_fullStr Diiron centre mutations in Ciona intestinalis alternative oxidase abolish enzymatic activity and prevent rescue of cytochrome oxidase deficiency in flies
title_full_unstemmed Diiron centre mutations in Ciona intestinalis alternative oxidase abolish enzymatic activity and prevent rescue of cytochrome oxidase deficiency in flies
title_sort Diiron centre mutations in Ciona intestinalis alternative oxidase abolish enzymatic activity and prevent rescue of cytochrome oxidase deficiency in flies
author Andjelkovic, Ana
author_facet Andjelkovic, Ana
Oliveira, Marcos T. [UNESP]
Cannino, Giuseppe
Yalgin, Cagri
Dhandapani, Praveen K.
Dufour, Eric
Rustin, Pierre
Szibor, Marten
Jacobs, Howard T.
author_role author
author2 Oliveira, Marcos T. [UNESP]
Cannino, Giuseppe
Yalgin, Cagri
Dhandapani, Praveen K.
Dufour, Eric
Rustin, Pierre
Szibor, Marten
Jacobs, Howard T.
author2_role author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Tampere Univ
Universidade Estadual Paulista (Unesp)
Univ Helsinki
INSERM
Universidade de São Paulo (USP)
dc.contributor.author.fl_str_mv Andjelkovic, Ana
Oliveira, Marcos T. [UNESP]
Cannino, Giuseppe
Yalgin, Cagri
Dhandapani, Praveen K.
Dufour, Eric
Rustin, Pierre
Szibor, Marten
Jacobs, Howard T.
description The 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.
publishDate 2015
dc.date.none.fl_str_mv 2015-12-17
2018-11-26T16:18:57Z
2018-11-26T16:18:57Z
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://dx.doi.org/10.1038/srep18295
Scientific Reports. London: Nature Publishing Group, v. 5, 9 p., 2015.
2045-2322
http://hdl.handle.net/11449/161054
10.1038/srep18295
WOS:000366569400001
WOS000366569400001.pdf
url http://dx.doi.org/10.1038/srep18295
http://hdl.handle.net/11449/161054
identifier_str_mv Scientific Reports. London: Nature Publishing Group, v. 5, 9 p., 2015.
2045-2322
10.1038/srep18295
WOS:000366569400001
WOS000366569400001.pdf
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Scientific Reports
1,533
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 9
application/pdf
dc.publisher.none.fl_str_mv Nature Publishing Group
publisher.none.fl_str_mv Nature Publishing Group
dc.source.none.fl_str_mv Web of Science
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv
_version_ 1808128359510573056

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