Iron-sulfur protein biogenesis in eukaryotes: components and mechanisms.
Iron-sulfur (Fe/S) clusters require a complex set of proteins to become assembled and incorporated into apoproteins in a living cell. Researchers have described three distinct assembly systems in eukaryotes that are involved in the maturation of cellular Fe/S proteins. Mitochondria are central for biogenesis. They contain the ISC-the iron-sulfur cluster assembly machinery that was inherited from a similar system of eubacteria in evolution and is involved in biogenesis of all cellular Fe/S proteins. The basic principle of mitochondrial (and bacterial) Fe/S protein maturation is the synthesis of the Fe/S cluster on a scaffold protein before the cluster is transferred to apoproteins. Biogenesis of cytosolic and nuclear Fe/S proteins is facilitated by the cytosolic iron-sulfur protein assembly (CIA) apparatus. This process requires the participation of mitochondria that export a still unknown component via the ISC export machinery, including an ABC transporter.
Lill
Roland
R
Institut für Zytobiologie, Philipps Universität Marburg, 35037 Marburg, Germany. lill@staff.uni-marburg.de
Mühlenhoff
Ulrich
U
D000818:Animals; D001419:Bacteria / Q000378:metabolism; D005057:Eukaryotic Cells / Q000378:metabolism*; D005287:Ferredoxin-NADP Reductase / Q000378:metabolism; D007506:Iron-Sulfur Proteins / Q000096:biosynthesis* / Q000378:metabolism; D008928:Mitochondria / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000378:metabolism
D007506:Iron-Sulfur Proteins; D005287:Ferredoxin-NADP Reductase