Reference: Zhang Y, et al. (2008) Dre2, a conserved eukaryotic fe/s cluster protein, functions in cytosolic fe/s protein biogenesis. Mol Cell Biol 28(18):5569-82

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Abstract

In a forward genetic screen for interaction with mitochondrial iron carrier proteins in yeast, a hypomorphic mutation of the essential DRE2 gene was found to confer lethality when combined with Deltamrs3 and Deltamrs4. 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 perfectly aligned. The human Dre2 homolog (implicated in blocking apoptosis and called CIAPIN1 or anamorsin) was able to complement the non-viability of a Deltadre2 deletion strain. The Dre2 protein with HA3 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 EPR 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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Journal Article
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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, ... Show all
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