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

Autor: Andjelković A; BioMediTech and Tampere University Hospital, University of Tampere, FI-33014, Finland., Oliveira MT; BioMediTech and Tampere University Hospital, University of Tampere, FI-33014, Finland.; Departamento de Tecnologia, Faculdade de Ciências Agrárias e Veterinárias, Universidade Estadual Paulista 'Júlio de Mesquita Filho', 14884-900 Jaboticabal, SP, Brazil., Cannino G; BioMediTech and Tampere University Hospital, University of Tampere, FI-33014, Finland., Yalgin C; BioMediTech and Tampere University Hospital, University of Tampere, FI-33014, Finland., Dhandapani PK; BioMediTech and Tampere University Hospital, University of Tampere, FI-33014, Finland.; Institute of Biotechnology, University of Helsinki, FI-00014, Finland., Dufour E; BioMediTech and Tampere University Hospital, University of Tampere, FI-33014, Finland., Rustin P; INSERM UMR 1141 and Université Paris 7, Faculté de Médecine Denis Diderot, Hôpital Robert Debré, 48, Boulevard Sérurier, 75019, Paris, France., Szibor M; BioMediTech and Tampere University Hospital, University of Tampere, FI-33014, Finland.; Institute of Biotechnology, University of Helsinki, FI-00014, Finland., Jacobs HT; BioMediTech and Tampere University Hospital, University of Tampere, FI-33014, Finland.; Institute of Biotechnology, University of Helsinki, FI-00014, Finland.
Jazyk: angličtina
Zdroj: Scientific reports [Sci Rep] 2015 Dec 17; Vol. 5, pp. 18295. Date of Electronic Publication: 2015 Dec 17.
DOI: 10.1038/srep18295
Abstrakt: 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.
Databáze: MEDLINE