The nuclear origin of the non-phosphorylating NADH dehydrogenases of plant mitochondria

R. J. Cook-Johnson, Q. Zhang, J. T. Wiskich, K. L. Soole

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    The oxidation of matrix and cytosolic NADH by isolated beetroot and wheat leaf mitochondria was investigated to determine whether the rotenone-insensitive NADH dehydrogenases of plant mitochondria were the products of nuclear or mitochondrial genes. After aging beetroot tissue (slicing and incubating in a CaSO4 solution), the induction of the level of matrix NADH oxidation in the presence of rotenone was greatly reduced in mitochondria isolated from tissue treated with cycloheximide, a nuclear protein synthesis inhibitor. This was also true for the oxidation of cytosolic NADH. Mitochondria isolated from chloramphenicol-treated tissue exhibited greatly increased levels of both matrix and external rotenone-insensitive NADH oxidation when compared to the increase due to the aging process alone. This increase was not accompanied by an increase in matrix NAD-linked substrate dehydrogenases such as malic enzyme nor intra-mitochondrial NAD levels. Possible explanations for this increase in rotenone-insensitive NADH oxidation are discussed. Based on these results we have concluded that the matrix facing rotenone-insensitive NADH dehydrogenase of plant mitochondria is encoded by a nuclear gene and synthesis of the protein occurs in the cytosol. Copyright (C) 1999 Federation of European Biochemical Societies.

    Original languageEnglish
    Pages (from-to)37-41
    Number of pages5
    JournalFEBS Letters
    Issue number1-2
    Publication statusPublished - 2 Jul 1999

    Bibliographical note

    Funding Information:
    The financial support for this work was from the Australian Research Council to K.L.S. and J.T.W.


    • Mitochondrion
    • NADH oxidation
    • Protein synthesis inhibition
    • Rotenone-insensitive


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