Reference : Characterization of two genes encoding the mitochondrial alternative oxidase in Chlamydo...
Scientific journals : Article
Life sciences : Phytobiology (plant sciences, forestry, mycology...)
Life sciences : Biochemistry, biophysics & molecular biology
Life sciences : Microbiology
Life sciences : Genetics & genetic processes
http://hdl.handle.net/2268/73236
Characterization of two genes encoding the mitochondrial alternative oxidase in Chlamydomonas reinhardtii
English
Dinant, Monique* [Université de Liège - ULg > Département de Botanique > Génétique des microorganismes > >]
Baurain, Denis* mailto [Université de Liège - ULg > Département de Botanique > Génétique des microorganismes > >]
Coosemans, Nadine mailto [Université de Liège - ULg > Département de Botanique > Génétique des microorganismes > >]
Joris, Bernard mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Matagne, René-Fernand mailto [Université de Liège - ULg > Département de Botanique > Génétique des microorganismes > >]
* These authors have contributed equally to this work.
Apr-2001
Current Genetics
39
2
101-108
Yes
International
0172-8083
[en] Two cDNA clones (AOX1 and AOX2) and the corresponding genes encoding the alternative oxidases (AOXs) from Chlamydomonas reinhardtii were isolated and sequenced. The cDNAs, AOX1 and AOX2, contained open reading frames (ORFs) encoding putative proteins of 360 amino acids and 347 amino acids, respectively. For each of the ORFs, a potential mitochondrial-targeting sequence was found in the 5'-end regions. In comparison to AOX enzymes from plants and fungi, the predicted amino acid sequences of the ORFs showed their highest degree of identity with proteins from Aspergillus niger (38.1% and 37.2%) and Ajellomyces capsulatus (37% and 34.9%). Several residues supposed either to be Fe ligands or to be involved in the ubiquinol-binding site were fully conserved in both C. reinhardtii putative AOX proteins. In contrast, a cysteine residue conserved in the sequences of all higher plants and probably involved in the regulation of the enzyme activity was missing both from the AOX1 and AOX2 amino acid sequences and from protein sequences from various other microorganisms. The transcriptional expression of the AOX1 and AOX2 genes in wild-type cells and in mutant cells deficient in mitochondrial complex III activity was also investigated.
http://hdl.handle.net/2268/73236
http://www.springerlink.com/content/hfqyy08r2klxfewt/
The original publication is available at www.springerlink.com

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