Abstract:
:Activity 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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Crichton PG,Affourtit C,Albury MS,Carré JE,Moore ALdoi
10.1016/j.febslet.2004.10.107keywords:
subject
Has Abstractpub_date
2005-01-17 00:00:00pages
331-6issue
2eissn
0014-5793issn
1873-3468pii
S0014-5793(04)01501-7journal_volume
579pub_type
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