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

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 Lett

journal_title

FEBS letters

authors

Crichton PG,Affourtit C,Albury MS,Carré JE,Moore AL

doi

10.1016/j.febslet.2004.10.107

keywords:

subject

Has Abstract

pub_date

2005-01-17 00:00:00

pages

331-6

issue

2

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(04)01501-7

journal_volume

579

pub_type

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