Dre2, a conserved eukaryotic Fe/S cluster protein, functions in cytosolic Fe/S protein biogenesis

Yan Zhang, Elise R. Lyver, Eiko Nakamaru-Ogiso, Heeyong Yoon, Boominathan Amutha, Dong Woo Lee, Erfei Bi, Tomoko Ohnishi, Fevzi Daldal, Debkumar Pain, Andrew Dancis

Research output: Contribution to journalArticle

114 Citations (Scopus)

Abstract

In a forward genetic screen for interaction with mitochondrial iron carrier proteins in Saccharomyces cerevisiae, a hypomorphic mutation of the essential DRE2 gene was found to confer lethality when combined with Δmrs3 and Δmrs4. The dre2 mutant or Dre2-depleted cells were deficient in cytosolic Fe/S cluster protein activities while maintaining mitochondrial Fe/S clusters. The Dre2 amino acid sequence was evolutionarily conserved, and cysteine motifs (CX2CXC and twin CX2C) in human and yeast proteins were perfectly aligned. The human Dre2 homolog (implicated in blocking apoptosis and called CIAPIN1 or anamorsin) was able to complement the nonviability of a Δdre2 deletion strain. The Dre2 protein with triple hemagglutinin tag was located in the cytoplasm and in the mitochondrial intermembrane space. Yeast Dre2 overexpressed and purified from bacteria was brown and exhibited signature absorption and electron paramagnetic resonance spectra, indicating the presence of both [2Fe-2S] and [4Fe-4S] clusters. Thus, Dre2 is an essential conserved Fe/S cluster protein implicated in extramitochondrial Fe/S cluster assembly, similar to other components of the so-called CIA (cytoplasmic Fe/S cluster assembly) pathway although partially localized to the mitochondrial intermembrane space.

Original languageEnglish
Pages (from-to)5569-5582
Number of pages14
JournalMolecular and Cellular Biology
Volume28
Issue number18
DOIs
Publication statusPublished - 2008 Sep 1

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Protein S
Fungal Proteins
Essential Genes
Electron Spin Resonance Spectroscopy
Hemagglutinins
Cysteine
Saccharomyces cerevisiae
Amino Acid Sequence
Carrier Proteins
Cytoplasm
Iron
Yeasts
Apoptosis
Bacteria
Mutation
Proteins

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

Cite this

Zhang, Yan ; Lyver, Elise R. ; Nakamaru-Ogiso, Eiko ; Yoon, Heeyong ; Amutha, Boominathan ; Lee, Dong Woo ; Bi, Erfei ; Ohnishi, Tomoko ; Daldal, Fevzi ; Pain, Debkumar ; Dancis, Andrew. / Dre2, a conserved eukaryotic Fe/S cluster protein, functions in cytosolic Fe/S protein biogenesis. In: Molecular and Cellular Biology. 2008 ; Vol. 28, No. 18. pp. 5569-5582.
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abstract = "In a forward genetic screen for interaction with mitochondrial iron carrier proteins in Saccharomyces cerevisiae, a hypomorphic mutation of the essential DRE2 gene was found to confer lethality when combined with Δmrs3 and Δmrs4. The dre2 mutant or Dre2-depleted cells were deficient in cytosolic Fe/S cluster protein activities while maintaining mitochondrial Fe/S clusters. The Dre2 amino acid sequence was evolutionarily conserved, and cysteine motifs (CX2CXC and twin CX2C) in human and yeast proteins were perfectly aligned. The human Dre2 homolog (implicated in blocking apoptosis and called CIAPIN1 or anamorsin) was able to complement the nonviability of a Δdre2 deletion strain. The Dre2 protein with triple hemagglutinin tag was located in the cytoplasm and in the mitochondrial intermembrane space. Yeast Dre2 overexpressed and purified from bacteria was brown and exhibited signature absorption and electron paramagnetic resonance spectra, indicating the presence of both [2Fe-2S] and [4Fe-4S] clusters. Thus, Dre2 is an essential conserved Fe/S cluster protein implicated in extramitochondrial Fe/S cluster assembly, similar to other components of the so-called CIA (cytoplasmic Fe/S cluster assembly) pathway although partially localized to the mitochondrial intermembrane space.",
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Zhang, Y, Lyver, ER, Nakamaru-Ogiso, E, Yoon, H, Amutha, B, Lee, DW, Bi, E, Ohnishi, T, Daldal, F, Pain, D & Dancis, A 2008, 'Dre2, a conserved eukaryotic Fe/S cluster protein, functions in cytosolic Fe/S protein biogenesis', Molecular and Cellular Biology, vol. 28, no. 18, pp. 5569-5582. https://doi.org/10.1128/MCB.00642-08

Dre2, a conserved eukaryotic Fe/S cluster protein, functions in cytosolic Fe/S protein biogenesis. / Zhang, Yan; Lyver, Elise R.; Nakamaru-Ogiso, Eiko; Yoon, Heeyong; Amutha, Boominathan; Lee, Dong Woo; Bi, Erfei; Ohnishi, Tomoko; Daldal, Fevzi; Pain, Debkumar; Dancis, Andrew.

In: Molecular and Cellular Biology, Vol. 28, No. 18, 01.09.2008, p. 5569-5582.

Research output: Contribution to journalArticle

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T1 - Dre2, a conserved eukaryotic Fe/S cluster protein, functions in cytosolic Fe/S protein biogenesis

AU - Zhang, Yan

AU - Lyver, Elise R.

AU - Nakamaru-Ogiso, Eiko

AU - Yoon, Heeyong

AU - Amutha, Boominathan

AU - Lee, Dong Woo

AU - Bi, Erfei

AU - Ohnishi, Tomoko

AU - Daldal, Fevzi

AU - Pain, Debkumar

AU - Dancis, Andrew

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N2 - In a forward genetic screen for interaction with mitochondrial iron carrier proteins in Saccharomyces cerevisiae, a hypomorphic mutation of the essential DRE2 gene was found to confer lethality when combined with Δmrs3 and Δmrs4. The dre2 mutant or Dre2-depleted cells were deficient in cytosolic Fe/S cluster protein activities while maintaining mitochondrial Fe/S clusters. The Dre2 amino acid sequence was evolutionarily conserved, and cysteine motifs (CX2CXC and twin CX2C) in human and yeast proteins were perfectly aligned. The human Dre2 homolog (implicated in blocking apoptosis and called CIAPIN1 or anamorsin) was able to complement the nonviability of a Δdre2 deletion strain. The Dre2 protein with triple hemagglutinin tag was located in the cytoplasm and in the mitochondrial intermembrane space. Yeast Dre2 overexpressed and purified from bacteria was brown and exhibited signature absorption and electron paramagnetic resonance spectra, indicating the presence of both [2Fe-2S] and [4Fe-4S] clusters. Thus, Dre2 is an essential conserved Fe/S cluster protein implicated in extramitochondrial Fe/S cluster assembly, similar to other components of the so-called CIA (cytoplasmic Fe/S cluster assembly) pathway although partially localized to the mitochondrial intermembrane space.

AB - In a forward genetic screen for interaction with mitochondrial iron carrier proteins in Saccharomyces cerevisiae, a hypomorphic mutation of the essential DRE2 gene was found to confer lethality when combined with Δmrs3 and Δmrs4. The dre2 mutant or Dre2-depleted cells were deficient in cytosolic Fe/S cluster protein activities while maintaining mitochondrial Fe/S clusters. The Dre2 amino acid sequence was evolutionarily conserved, and cysteine motifs (CX2CXC and twin CX2C) in human and yeast proteins were perfectly aligned. The human Dre2 homolog (implicated in blocking apoptosis and called CIAPIN1 or anamorsin) was able to complement the nonviability of a Δdre2 deletion strain. The Dre2 protein with triple hemagglutinin tag was located in the cytoplasm and in the mitochondrial intermembrane space. Yeast Dre2 overexpressed and purified from bacteria was brown and exhibited signature absorption and electron paramagnetic resonance spectra, indicating the presence of both [2Fe-2S] and [4Fe-4S] clusters. Thus, Dre2 is an essential conserved Fe/S cluster protein implicated in extramitochondrial Fe/S cluster assembly, similar to other components of the so-called CIA (cytoplasmic Fe/S cluster assembly) pathway although partially localized to the mitochondrial intermembrane space.

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