Characterization of mitochondrial ferritin in <i>Drosophila</i>

DOI Web Site 被引用文献4件
  • Fanis Missirlis
    *Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892; and
  • Sara Holmberg
    *Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892; and
  • Teodora Georgieva
    Department of Biochemistry and Molecular Biophysics and Center for Insect Science, University of Arizona, Tucson, AZ 85721
  • Boris C. Dunkov
    Department of Biochemistry and Molecular Biophysics and Center for Insect Science, University of Arizona, Tucson, AZ 85721
  • Tracey A. Rouault
    *Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892; and
  • John H. Law
    Department of Biochemistry and Molecular Biophysics and Center for Insect Science, University of Arizona, Tucson, AZ 85721

説明

<jats:p> Mitochondrial function depends on iron-containing enzymes and proteins, whose maturation requires available iron for biosynthesis of iron–sulfur clusters and heme. Little is known about how mitochondrial iron homeostasis is maintained, although the recent discovery of a mitochondrial ferritin in mammals and plants has uncovered a potential key player in the process. Here, we show that <jats:italic>Drosophila melanogaster</jats:italic> expresses mitochondrial ferritin from an intron-containing gene. It has high similarity to the mouse and human mitochondrial ferritin sequences and, as in mammals, is expressed mainly in testis. This ferritin contains a putative mitochondrial targeting sequence and an epitope-tagged version localizes to mitochondria in transfected cells. Overexpression of mitochondrial ferritin fails to alter both total-body iron levels and iron that is bound to secretory ferritins. However, the viability of iron-deficient flies is compromised by overexpression of mitochondrial ferritin, suggesting that it may sequester iron at the expense of other important cellular functions. The conservation of mitochondrial ferritin in an insect species underscores the importance of this iron-storage molecule. </jats:p>

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