About: Human mitochondrial ferritin improves respiratory function in yeast mutants deficient in iron-sulfur cluster biogenesis, but is not a functional homologue of yeast frataxin     Goto   Sponge   NotDistinct   Permalink

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Description
  • We overexpressed human mitochondrial ferritin in frataxin-deficient yeast cells (yfh1), but also in another mutant affected in [Fe-S] assembly (ggc1). Ferritin was correctly processed and expressed in the mitochondria of these cells, but the fraction of total mitochondrial iron bound to ferritin was very low, and most of the iron remained in the form of insoluble particles of ferric phosphate in these mitochondria, as evidenced by gel filtration analysis of the mitochondrial matrix (fast protein liquid chromatography [FPLC]) and by Mossbauer spectroscopy. Mutant cells in which ferritin was overexpressed still accumulated iron in the mitochondria and remained deficient in [Fe-S] assembly, suggesting that human mitochondrial ferritin is not a functional homologue of yeast frataxin. However, the respiratory function was improved in these mutants, which correlates with an improvement of cytochrome and heme synthesis.Overexpression of mitochondrial ferritin in [Fe-S] mutants resulted in the appearance of a small pool of high-spin ferrous iron in the mitochondria, which was probably responsible for the improvement of heme synthesis and of the respiratory function in these mutants.
  • We overexpressed human mitochondrial ferritin in frataxin-deficient yeast cells (yfh1), but also in another mutant affected in [Fe-S] assembly (ggc1). Ferritin was correctly processed and expressed in the mitochondria of these cells, but the fraction of total mitochondrial iron bound to ferritin was very low, and most of the iron remained in the form of insoluble particles of ferric phosphate in these mitochondria, as evidenced by gel filtration analysis of the mitochondrial matrix (fast protein liquid chromatography [FPLC]) and by Mossbauer spectroscopy. Mutant cells in which ferritin was overexpressed still accumulated iron in the mitochondria and remained deficient in [Fe-S] assembly, suggesting that human mitochondrial ferritin is not a functional homologue of yeast frataxin. However, the respiratory function was improved in these mutants, which correlates with an improvement of cytochrome and heme synthesis.Overexpression of mitochondrial ferritin in [Fe-S] mutants resulted in the appearance of a small pool of high-spin ferrous iron in the mitochondria, which was probably responsible for the improvement of heme synthesis and of the respiratory function in these mutants. (en)
Title
  • Human mitochondrial ferritin improves respiratory function in yeast mutants deficient in iron-sulfur cluster biogenesis, but is not a functional homologue of yeast frataxin
  • Human mitochondrial ferritin improves respiratory function in yeast mutants deficient in iron-sulfur cluster biogenesis, but is not a functional homologue of yeast frataxin (en)
skos:prefLabel
  • Human mitochondrial ferritin improves respiratory function in yeast mutants deficient in iron-sulfur cluster biogenesis, but is not a functional homologue of yeast frataxin
  • Human mitochondrial ferritin improves respiratory function in yeast mutants deficient in iron-sulfur cluster biogenesis, but is not a functional homologue of yeast frataxin (en)
skos:notation
  • RIV/00216208:11310/12:10129874!RIV13-MSM-11310___
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • I, Z(MSM0021620858)
http://linked.open...iv/cisloPeriodika
  • 2
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
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  • 139875
http://linked.open...ai/riv/idVysledku
  • RIV/00216208:11310/12:10129874
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • yfh1; yeast frataxin; Mossbauer; mitochondria, mitochondrial; iron; ggc1; Ferritin (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • GB - Spojené království Velké Británie a Severního Irska
http://linked.open...ontrolniKodProRIV
  • [28C886667E92]
http://linked.open...i/riv/nazevZdroje
  • MicrobiologyOpen [online]
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
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http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 1
http://linked.open...iv/tvurceVysledku
  • Tachezy, Jan
  • Šuťák, Róbert
  • Camadro, Jean-Michel
  • Lesuisse, Emmanuel
  • Dancis, Andrew
  • Garcia-Serres, Ricardo
  • Latour, Jean-Marc
  • Oddou, Jean-Louis
  • Seguin, Alexandra
http://linked.open...n/vavai/riv/zamer
issn
  • 2045-8827
number of pages
http://bibframe.org/vocab/doi
  • 10.1002/mbo3.18
http://localhost/t...ganizacniJednotka
  • 11310
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