Response of mitochondria to light intensity in the leaves of sun and shade species

Authors

  • KO NOGUCHI,

    Corresponding author
    1. Department of Biology, Graduate School of Science, Osaka University, 1–1 Machikaneyama-Cho, Toyonaka, Osaka, 560–0043, Japan,
    2. Biochemistry and Molecular Biology, School of Biomedical and Chemical Sciences and
    3. School of Plant Biology, the University of Western Australia, Australia
      Ko Noguchi. Fax: + 81 6 6850 5808; e-mail: address: knoguchi@bio.sci.osaka-u.ac.jp
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  • NICOLAS L. TAYLOR,

    1. Biochemistry and Molecular Biology, School of Biomedical and Chemical Sciences and
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  • A. HARVEY MILLAR,

    1. Biochemistry and Molecular Biology, School of Biomedical and Chemical Sciences and
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  • HANS LAMBERS,

    1. School of Plant Biology, the University of Western Australia, Australia
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  • DAVID A. DAY

    1. Biochemistry and Molecular Biology, School of Biomedical and Chemical Sciences and
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Ko Noguchi. Fax: + 81 6 6850 5808; e-mail: address: knoguchi@bio.sci.osaka-u.ac.jp

ABSTRACT

The present authors have shown previously that both respiration rates and in vivo activities of the alternative oxidase (AOX) of leaves of Alocasia odora, a shade species, are lower than those in sun species, thereby optimizing energy production under limited light conditions (Noguchi et al., Australian Journal of Plant Physiology 28, 27–35, 2001). In the present study, mitochondria isolated from A. odora leaves were examined in order to investigate the biochemical basis for the differences in respiratory parameters. Alocasia odora and spinach plants were cultivated under both high and low light intensities, mitochondria were isolated from their leaves, and their respiratory properties compared. Mitochondrial content of leaf extracts from the two species was estimated using fumarase activities and antibody detection of porin (the voltage-dependent anion channel of the outer mitochondrial membrane). On a mitochondrial protein basis, spinach leaves showed higher capacities of the cytochrome pathway and cytochrome c oxidase (COX) than A. odora leaves. However, on a mitochondrial protein basis, A. odora showed higher capacities of AOX, which had a high affinity for ubiquinone when activated by pyruvate. Alocasia odora also had larger amounts of mitochondrial protein per leaf dry weight, even under severely shaded conditions, than spinach. Lower growth light intensity led to lower activities of most pathways and proteins tested in both species, especially glycine-dependent oxygen uptake. In the low light environment, most of the AOX protein in A. odora leaves was in its inactive, oxidized dimer form, but was converted to its reduced active form when plants were grown under high light. This shift may prevent over-reduction of the respiratory chain under photo-oxidative conditions.

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