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An essential function of the mitochondrial sulfhydryl oxidase Erv1p/ALR in the maturation of cytosolic Fe/S proteins
Author(s) -
Lange Heike,
Lisowsky Thomas,
Gerber Jana,
Mühlenhoff Ulrich,
Kispal Gyula,
Lill Roland
Publication year - 2001
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1093/embo-reports/kve161
Subject(s) - cytosol , mitochondrion , mitochondrial intermembrane space , biogenesis , intermembrane space , microbiology and biotechnology , biology , mitochondrial biogenesis , biochemistry , compartment (ship) , mitochondrial carrier , protein targeting , saccharomyces cerevisiae , membrane protein , yeast , bacterial outer membrane , enzyme , gene , escherichia coli , membrane , geology , oceanography
Biogenesis of Fe/S clusters involves a number of essential mitochondrial proteins. Here, we identify the essential Erv1p of Saccharomyces cerevisia mitochondria as a novel component that is specifically required for the maturation of Fe/S proteins in the cytosol, but not in mitochondria. Furthermore, Erv1p was found to be important for cellular iron homeostasis. The homologous mammalian protein ALR (‘augmenter of liver regeneration’), also termed hepatopoietin, can functionally replace defects in Erv1p and thus represents the mammalian orthologue of yeast Erv1p. Previously, a fragment of ALR was reported to exhibit an activity as an extracellular hepatotrophic growth factor. Both Erv1p and full‐length ALR are located in the mitochondrial intermembrane space and represent the first components of this compartment with a role in the biogenesis of cytosolic Fe/S proteins. It is likely that Erv1p/ALR operates downstream of the mitochondrial ABC transporter Atm1p/ABC7/Sta1, which also executes a specific task in this essential biochemical process.