The chemical versatility inherent in Fe-S clusters allow these cofactors, when bound to their partner proteins, to play a direct role in several diverse biochemical processes including respiration, photosynthesis and RNA/DNA production/modification/repair.  During regulation, these Fe-cofactors can modulate the activity of their regulatory protein partner by serving in a structural, catalytic or electron transfer role.  Activation of the Fe-S cluster containing regulatory protein is initiated by the bioassembly of this essential Fe cofactor, and the bulk of the eukaryotic Fe-S clusters are produced within the mitochondria.  The highly coordinated activity of the mitochondrial Fe-S cluster (ISC) assembly apparatus of proteins, which in yeast includes the assembly scaffold protein (Isu1), the cysteine desulfurase (Nfs1) the NFS accessory protein (Isd11), the ferrodoxin (Yah1) and the assembly/Fe delivery regulatory protein frataxin (Yfh1), work together to meet the bulk of the cellular Fe-S cluster demands, and also trigger the export of the mitochondrially produced S-molecule that triggers Fe-S cluster assembly in the cytosol.  This coordinated pathway for Fe homeostasis in under investigation by our laboratory.<br/> <br/>      Using the yeast model system, our laboratory has prepared and characterized all protein partners in the ISC cluster assembly pathway.  Anaerobic spectroscopic and thermodynamic analysis (CD, ITC, DSC, XAS) has been used to characterize the structure and function of iron during assembly and the molecular activities of the protein partners during coordinated Fe-S cluster bioproduction events.   Our model for assembly and the early stages for delivery of clusters for eventual incorporation into gene regulation proteins will be discussed.   <br/>

Fe-S cluster biosynthesis provides cofactors to activate proteins that drive gene regulation

251st National Meeting (2016)

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