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

Result code in 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>

Result on the web

<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>

Result language

angličtina

Original language name

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

Original language 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 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

Czech name

—

Czech description

—

Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

EB - Genetics and molecular biology

OECD FORD branch

—

Project

—

Continuities

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

Publication year

2012

Confidentiality

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

Name of the periodical

MicrobiologyOpen [online]

ISSN

2045-8827

e-ISSN

—

Volume of the periodical

1

Issue of the periodical within the volume

2

Country of publishing house

GB - UNITED KINGDOM

Number of pages

9

Pages from-to

95-104

UT code for WoS article

—

EID of the result in the Scopus database

—