The ABC transport Atm1p is required for mitochondrial iron homeostasis

G. Kispál, Peter Csere, Bernard Guiard, Roland Lill

Research output: Contribution to journalArticle

216 Citations (Scopus)

Abstract

The function of the ABC transporter Atm1p located in the mitochondrial inner membrane is not yet known. To study its cellular role, we analyzed a mutant in which ATM1 was disrupted, Δatm1 cells are deficient in the holoforms, but not the apoforms of heme-carrying proteins both within and outside mitochondria, yet both synthesis and transport of heme are functional, Δatm1 cells are hypersensitive for growth in the presence of oxidative reagents, and they contain increased levels of the antioxidant glutathione, in particular of its oxidized form. Mitochondria deficient in Atm1p accumulate 30-fold higher levels of free iron as compared to wild-type organelles, i.e. threefold more than mitochondria deficient in frataxin, the protein mutated in Friedreich's ataxia. The increased mitochondrial iron content may be causative of the oxidative damage of heme-containing proteins in Δatm1 cells. Our data assign an important function to Atm1p in mitochondrial iron homeostasis.

Original languageEnglish
Pages (from-to)346-350
Number of pages5
JournalFEBS Letters
Volume418
Issue number3
DOIs
Publication statusPublished - Dec 1 1997

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Mitochondria
Heme
Homeostasis
Iron
Friedreich Ataxia
Proteins
ATP-Binding Cassette Transporters
Mitochondrial Membranes
Organelles
Glutathione
Antioxidants
Membranes
Growth

Keywords

  • ABC transporter
  • Mitochondrial iron homeostasis

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

The ABC transport Atm1p is required for mitochondrial iron homeostasis. / Kispál, G.; Csere, Peter; Guiard, Bernard; Lill, Roland.

In: FEBS Letters, Vol. 418, No. 3, 01.12.1997, p. 346-350.

Research output: Contribution to journalArticle

Kispál, G. ; Csere, Peter ; Guiard, Bernard ; Lill, Roland. / The ABC transport Atm1p is required for mitochondrial iron homeostasis. In: FEBS Letters. 1997 ; Vol. 418, No. 3. pp. 346-350.
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