Diiron centre mutations in Ciona intestinalis alternative oxidase abolish enzymatic activity and prevent rescue of cytochrome oxidase deficiency in flies
Andjelković, Ana; Oliveira, Marcos T; Guiseppe, Cannino; Yalgin, Cagri; Dhandapani, Praveen K; Dufour, Eric; Rustin, Pierre; Szibor, Marten; Jacobs, Howard T (2015)
Andjelković, Ana
Oliveira, Marcos T
Guiseppe, Cannino
Yalgin, Cagri
Dhandapani, Praveen K
Dufour, Eric
Rustin, Pierre
Szibor, Marten
Jacobs, Howard T
2015
Scientific Reports 5
18295
BioMediTech - BioMediTech
Julkaisun pysyvä osoite on
https://urn.fi/URN:NBN:fi:uta-201608042131
https://urn.fi/URN:NBN:fi:uta-201608042131
Tiivistelmä
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.
Kokoelmat
- Artikkelit [6140]