Journal
BIOLOGICAL CHEMISTRY
Volume 401, Issue 6-7, Pages 855-876Publisher
WALTER DE GRUYTER GMBH
DOI: 10.1515/hsz-2020-0117
Keywords
ABC protein; CIA machinery; Fe/S cluster; Fe/S disease; ISC machinery; metallo proteins
Categories
Funding
- Deutsche Forschungsgemeinschaft [LI415/6, LI 415/5, SFB 987, SPP 1710, SPP 1927]
- German-Israeli Foundation GIF [I-1302-412.13/2015]
- COST Action FeSBioNet [CA15133]
- Volkswagen Foundation
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Protein cofactors often are the business ends of proteins, and are either synthesized inside cells or are taken up from the nutrition. A cofactor that strictly needs to be synthesized by cells is the iron-sulfur (Fe/S) cluster. This evolutionary ancient compound performs numerous biochemical functions including electron transfer, catalysis, sulfur mobilization, regulation and protein stabilization. Since the discovery of eukaryotic Fe/S protein biogenesis two decades ago, more than 30 biogenesis factors have been identified in mitochondria and cytosol. They support the synthesis, trafficking and target-specific insertion of Fe/S clusters. In this review, I first summarize what led to the initial discovery of Fe/S protein biogenesis in yeast. I then discuss the function and localization of Fe/S proteins in (non-green) eukaryotes. The major part of the review provides a detailed synopsis of the three major steps of mitochondrial Fe/S protein biogenesis, i.e. the de novo synthesis of a [2Fe-2S] cluster on a scaffold protein, the Hsp70 chaper-one-mediated transfer of the cluster and integration into [2Fe-2S] recipient apoproteins, and the reductive fusion of [2Fe-2S] to [4Fe-4S] clusters and their subsequent assembly into target apoproteins. Finally, I summarize the current knowledge of the mechanisms underlying the maturation of cytosolic and nuclear Fe/S proteins.
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