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

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F12%3A10129874" target="_blank" >RIV/00216208:11310/12:10129874 - isvavai.cz</a>

Výsledek na webu

<a href="http://onlinelibrary.wiley.com/doi/10.1002/mbo3.18/suppinfo" target="_blank" >http://onlinelibrary.wiley.com/doi/10.1002/mbo3.18/suppinfo</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/mbo3.18" target="_blank" >10.1002/mbo3.18</a>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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 oftotal 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 liquidchromatography [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 functionalhomologue 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

Název v anglickém jazyce

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

Popis výsledku anglicky

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 oftotal 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 liquidchromatography [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 functionalhomologue 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

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EB - Genetika a molekulární biologie

OECD FORD obor

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Projekt

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Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2012

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

MicrobiologyOpen [online]

ISSN

2045-8827

e-ISSN

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Svazek periodika

1

Číslo periodika v rámci svazku

2

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

9

Strana od-do

95-104

Kód UT WoS článku

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EID výsledku v databázi Scopus

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