Constitutive activity of Sauromatum guttatum alternative oxidase in Schizosaccharomyces pombe implicates residues in addition to conserved cysteines in α-keto acid activation

Crichton, Paul G. ORCID: https://orcid.org/0000-0003-3786-8359, Affourtit, Charles, Albury, Mary S., Carré, Jane E. and Moore, Anthony L. (2005) Constitutive activity of Sauromatum guttatum alternative oxidase in Schizosaccharomyces pombe implicates residues in addition to conserved cysteines in α-keto acid activation. FEBS Letters, 579 (2). pp. 331-336. ISSN 0014-5793

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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.

Item Type: Article
Uncontrolled Keywords: ccp,carbonyl cyanide m-chlorophenylhydrazone,q(h2),ubiquinol,alternative oxidase structure,regulation,pyruvate,plant respiration,s. pombe mitochondria
Faculty \ School: Faculty of Medicine and Health Sciences > Norwich Medical School
UEA Research Groups: Faculty of Medicine and Health Sciences > Research Groups > Cardiovascular and Metabolic Health
Faculty of Medicine and Health Sciences > Research Centres > Metabolic Health
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Depositing User: Pure Connector
Date Deposited: 03 Nov 2016 10:00
Last Modified: 19 Oct 2023 01:51
URI: https://ueaeprints.uea.ac.uk/id/eprint/61212
DOI: 10.1016/j.febslet.2004.10.107

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