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Constitutive activity of Sauromatum guttatum alternative oxidase in Schizosaccharomyces pombe implicates residues in addition to conserved cysteines in a-keto acid activation
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posted on 2023-06-08, 06:44 authored by Paul G Crichton, Charles Affourtit, Mary Albury, Jane E Carre, Anthony MooreActivity of the plant mitochondrial alternative oxidase (AOX) can be regulated by organic acids, notably pyruvate. To date, only two well-conserved cysteine residues have been implicated in this process. We report the functional expression of two AOX isozymes (Sauromatum guttatum Sg-AOX and Arabidopsis thaliana At-AOX1a) in Schizosaccharomyces pombe. Comparison of the response of these two isozymes to pyruvate in isolated yeast mitochondria and disrupted mitochondrial membranes reveals that in contrast to At-AOX1a, Sg-AOX activity is insensitive to pyruvate and appears to be in a constitutively active state. As both of these isozymes conserve the two cysteines, we propose that such contrasting behaviour must be a direct result of differences in their amino acid sequence and have subsequently identified novel candidate residues.
History
Publication status
- Published
Journal
FEBS LettersISSN
0014-5793External DOI
Issue
2Volume
579Page range
331-336Pages
6.0Department affiliated with
- Biochemistry Publications
Notes
All co-authors were postdocs in my lab where the research was carried out. Results demonstrate that constitutive alternative oxidase activity is not due to the presence of cysteines as previously proposed by others but due to upstream residues.Full text available
- No
Peer reviewed?
- Yes
Legacy Posted Date
2012-02-06Usage metrics
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