4Fe-4S cluster assembles on NUBP2:NUBP1 scaffold

Stable Identifier
R-HSA-2564826
Type
Reaction [omitted]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout
Mitochondria export via a mitochondrial ABC transporter (yeast ATM1, human ABCB7) a still unknown, sulfur-containing compound which is essential for Fe/S cluster assembly in the cytosol. As inferred from the yeast homolog Atm1p, the compound may be a 2Fe-2S cluster complexed with glutathione (Li and Cowan 2015) A [4Fe-4S] cluster is assembled on a scaffold composed of the P-loop NTPases NUBP2 (CFD1 in yeast) and NUBP1 (Nbp35 in yeast) in a nucleotide-dependent fashion. The two proteins form a heterotetramer which transiently binds the [4Fe-4S] cluster in a bridged form between two subunits of the complex. The Fe/S cluster is bound to two highly conserved Cys residues in the C-termini of each of these proteins. NUBP1 contains an additional, stably associated [4Fe-4S] cluster at its N-terminus which is essential for function.
Mitochondria play a crucial role in cytosolic and nuclear Fe/S protein biogenesis. They export via a mitochondrial ABC transporter (yeast ATM1, human ABCB7) a still unknown, sulfur-containing compound which is essential for Fe/S cluster assembly in the cytosol.
The general cytosolic iron donor, the multi-domain monothiol glutaredoxin (human GRX3 or PICOT, yeast Grx3-Grx4) plays a crucial role in cytosolic-nuclear Fe/S protein biogenesis. The precise molecular function of the glutaredoxin is still unclear.
Literature References
PubMed ID Title Journal Year
18573874 Human Nbp35 is essential for both cytosolic iron-sulfur protein assembly and iron homeostasis

Niggemeyer, B, Netz, DJ, Pierik, AJ, Lill, R, Puccio, H, Stehling, O, Eisenstein, RS, Rösser, R

Mol. Cell. Biol. 2008
Participants
Participates
Catalyst Activity

electron transfer activity of NDOR1:CIAPIN1 reduced [cytosol]

This event is regulated
Inferred From
Authored
Reviewed
Created
Cite Us!