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Furthermore, Erv1p was found to be important for cellular iron homeostasis. Paper-8920497.
Erv1p from Saccharomyces cerevisiae is a FAD-linked sulfhydryl oxidase. Paper-8409686.
Mia40 contains cysteine residues, which are oxidized by the sulfhydryl oxidase Erv1. Paper-11003976.
Erv1p is a FAD-dependent sulfhydryl oxidase of the mitochondrial intermembrane space. Paper-14041984.
The essential mitochondrial protein Erv1 cooperates with Mia40 in biogenesis of intermembrane space proteins. Paper-11457636.
Mitochondrial disulfide bond formation is driven by intersubunit electron transfer in Erv1 and proofread by glutathione. Paper-14649815.
An essential function of the mitochondrial sulfhydryl oxidase Erv1p/ALR in the maturation of cytosolic Fe/ S proteins. Paper-8920497.
ERV1 is involved in the cell-division cycle and the maintenance of mitochondrial genomes in Saccharomyces cerevisiae. Paper-140902.
Redox titrations of recombinant Erv1 showed that it contains three distinct couples with midpoint potentials of -320, -215, and -150 mV. Paper-12548201.
In former studies it was found that the ERV1 gene is essential for cell viability and for the biogenesis of functional mitochondria. Paper-140902.
Furthermore, we provide direct evidence for the intramolecular electron transfer from the shuttle cysteine pair of Erv1 to the core domain. Paper-15199079.
Both cysteine residues are required for the oxidation of the substrate, Tim10, in a reconstituted system comprised of Mia40 and Erv1. Paper-13570792.
This import pathway employs a disulfide relay system whose key components are the redox-regulated import receptor Mia40 and the thiol oxidase Erv1. Paper-13570792.
In the reconstituted system the thiol oxidase Erv1p was sufficient to transfer disulfide bonds to Mia40C, which then could oxidize the variant of Mia40C. Paper-13437396.
Erv1 is a flavin-dependent sulfhydryl oxidase in the mitochondrial intermembrane space (IMS) that functions in the import of cysteine-rich proteins. Paper-12548201.
Furthermore, the disulfide bond in the CPC segment mediates the redox reactions with the thiol oxidase Erv1 and substrate proteins in mitochondria. Paper-13570792.
This fragment of Erv1p still binds FAD and catalyzes the formation of disulfide bonds but is no longer able to form dimers like the complete protein. Paper-8409686.
Mia40p and Erv1p are components of a translocation pathway for the import of cysteine-rich proteins into the intermembrane space of mitochondria. Paper-13437396.
Thus Erv1p represents the first FAD-linked sulfhydryl oxidase from yeast and the first of these enzymes that is involved in mitochondrial biogenesis. Paper-8409686.
We have generated strains with erv1 conditional alleles and employed biochemical and genetic strategies to facilitate identifying redox pathways involving Erv1. Paper-12548201.
It is required for the interaction of Mia40 with Erv1 in a disulfide intermediate and forms a redox-sensitive disulfide bond with the first cysteine residue. Paper-13570792.
The N-terminal shuttle domain of Erv1 determines the affinity for Mia40 and mediates electron transfer to the catalytic Erv1 core in yeast mitochondria. Paper-15199079.
Erv1 and Mia40 constitute the two important components of the disulfide relay system that mediates oxidative protein folding in the mitochondrial intermembrane space. Paper-15199079.
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. Paper-8920497.
All of the mutants were purified with the normal FAD binding properties as the wild type Erv1p, showing that none of the three disulfides are essential for FAD binding. Paper-14041984.
However, efficient reoxidation of a Mia40C variant containing only the cysteine residues of the twin CX(9)C motif was observed when in addition to Erv1p low amounts of wild type Mia40C were present. Paper-13437396.
We have characterized the redox behavior of Mia40p and reconstituted the disulfide transfer system of Mia40p by using recombinant functional C-terminal fragment of Mia40p, Mia40C, and Erv1p. Paper-13437396.
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. Paper-8920497.
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. Paper-8920497.
Thus, we provided the first experimental evidence of electron transfer between the shuttle and active site disulfides of Erv1p, and we propose that both intersubunit and intermolecular electron transfer can occur. Paper-14041984.
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. Paper-8920497.
Here, we show that Erv1, a further essential IMS protein that has been reported to function as a sulfhydryl oxidase and participate in biogenesis of Fe/ S proteins, is also required for the biogenesis of small IMS proteins. Paper-11457636.
Our aims here were to dissect the domain of Erv1 that mediates the protein-protein interaction with Mia40 and to investigate the interactions between the shuttle domain of Erv1 and its catalytic core and their relevance for the interaction with Mia40. Paper-15199079.
These accession numbers are used for gene ERV1: .
ERV1 is a homologue of NCU02396 (augmenter of liver regeneration) from Neurospora crassa OR74A.
ERV1 is a homologue of MGG_13005 (hypothetical protein) from Magnaporthe oryzae 70-15.
ERV1 is a homologue of KLLA0B06061g (hypothetical protein) from Kluyveromyces lactis NRRL Y-1140.
ERV1 is a homologue of GFER (growth factor, augmenter of liver regeneration) from Homo sapiens.
ERV1 is a homologue of GFER (growth factor, augmenter of liver regeneration) from Pan troglodytes.
ERV1 is a homologue of GFER (growth factor, augmenter of liver regeneration) from Canis lupus familiaris.
ERV1 is a homologue of GFER (growth factor, augmenter of liver regeneration) from Bos taurus.
ERV1 is a homologue of GFER (growth factor, augmenter of liver regeneration (ERV1 homolog, S. cerevisiae)) from Gallus gallus.
ERV1 is a homologue of Gfer (growth factor, erv1 (S. cerevisiae)-like (augmenter of liver regeneration)) from Mus musculus.
ERV1 is a homologue of Gfer (growth factor, augmenter of liver regeneration) from Rattus norvegicus.
ERV1 is a homologue of gfer (growth factor, augmenter of liver regeneration (ERV1 homolog, S. cerevisiae)) from Danio rerio.
ERV1 is a homologue of F56C11.3 (hypothetical protein) from Caenorhabditis elegans.
ERV1 is a homologue of erv1 (sulfhydryl oxidase (predicted)) from Schizosaccharomyces pombe 972h-.
ERV1 is a homologue of Alr (Augmenter of liver regeneration) from Drosophila melanogaster.
ERV1 is a homologue of AGOS_ABR037W (ABR037Wp) from Ashbya gossypii ATCC 10895.
ERV1 is a homologue of AgaP_AGAP006470 (AGAP006470-PA) from Anopheles gambiae str. PEST.
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