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Elucidating the mitochondrial proteome of Toxoplasma gondii reveals the presence of a divergent cytochrome c oxidase.
Seidi, Azadeh; Muellner-Wong, Linden S; Rajendran, Esther; Tjhin, Edwin T; Dagley, Laura F; Aw, Vincent Yt; Faou, Pierre; Webb, Andrew I; Tonkin, Christopher J; van Dooren, Giel G.
Afiliação
  • Seidi A; Research School of Biology, Australian National University, Canberra, Australia.
  • Muellner-Wong LS; Research School of Biology, Australian National University, Canberra, Australia.
  • Rajendran E; Research School of Biology, Australian National University, Canberra, Australia.
  • Tjhin ET; Research School of Biology, Australian National University, Canberra, Australia.
  • Dagley LF; The Walter and Eliza Hall Institute of Medical Research, Victoria, Australia.
  • Aw VY; Department of Medical Biology, University of Melbourne, Victoria, Australia.
  • Faou P; Research School of Biology, Australian National University, Canberra, Australia.
  • Webb AI; Department of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Victoria, Australia.
  • Tonkin CJ; The Walter and Eliza Hall Institute of Medical Research, Victoria, Australia.
  • van Dooren GG; Department of Medical Biology, University of Melbourne, Victoria, Australia.
Elife ; 72018 09 11.
Article em En | MEDLINE | ID: mdl-30204084
ABSTRACT
The mitochondrion of apicomplexan parasites is critical for parasite survival, although the full complement of proteins that localize to this organelle has not been defined. Here we undertake two independent approaches to elucidate the mitochondrial proteome of the apicomplexan Toxoplasma gondii. We identify approximately 400 mitochondrial proteins, many of which lack homologs in the animals that these parasites infect, and most of which are important for parasite growth. We demonstrate that one such protein, termed TgApiCox25, is an important component of the parasite cytochrome c oxidase (COX) complex. We identify numerous other apicomplexan-specific components of COX, and conclude that apicomplexan COX, and apicomplexan mitochondria more generally, differ substantially in their protein composition from the hosts they infect. Our study highlights the diversity that exists in mitochondrial proteomes across the eukaryotic domain of life, and provides a foundation for defining unique aspects of mitochondrial biology in an important phylum of parasites.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Toxoplasma / Complexo IV da Cadeia de Transporte de Elétrons / Proteoma / Mitocôndrias Idioma: En Ano de publicação: 2018 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Toxoplasma / Complexo IV da Cadeia de Transporte de Elétrons / Proteoma / Mitocôndrias Idioma: En Ano de publicação: 2018 Tipo de documento: Article