NADPH reduces TAH18:DRE2

Stable Identifier
Reaction [dissociation]
Saccharomyces cerevisiae
SVG |   | PPTX  | SBGN
NADPH reduces TAH18:DRE2

Cytosolic Fe/S protein biogenesis depends on the electron transfer chain from NAD(P)H to the Fe/S protein Dre2 (human CIAPIN) via the flavoprotein Tah18 (human NDOR1). The precise role of electrons in the assembly process is unclear but in the absence of the electron chain the stable [4Fe-4S] cluster of Nbp35 is not assembled. Dre2 binds two Fe/S clusters of the [2Fe-2S] and the [4Fe-4S] type. The [2Fe-2S] cluster is reduced by Tah18-NADPH.

Literature References
PubMed ID Title Journal Year
20802492 Tah18 transfers electrons to Dre2 in cytosolic iron-sulfur protein biogenesis

Netz, DJ, Pierik, AJ, Doré, C, Lill, R, Stümpfig, M, Mühlenhoff, U

Nat. Chem. Biol. 2010
18625724 Dre2, a conserved eukaryotic Fe/S cluster protein, functions in cytosolic Fe/S protein biogenesis

Pain, D, Dancis, A, Lyver, ER, Bi, E, Daldal, F, Zhang, Y, Ohnishi, T, Yoon, H, Lee, DW, Amutha, B, Nakamaru-Ogiso, E

Mol. Cell. Biol. 2008
19194512 A newly identified essential complex, Dre2-Tah18, controls mitochondria integrity and cell death after oxidative stress in yeast

Baldacci, G, Guiard, B, Vernis, L, Faye, G, Chanet, R, Facca, C, Soler, N, Delagoutte, E

PLoS ONE 2009
Orthologous Events
Cite Us!