InterPro domain: IPR004640

The final step of iron-sulfur protein assembly involves transfer of an iron-sulfur cluster from a cluster-donor to a cluster-acceptor protein [ 1 ]. This process is facilitated by a specialized chaperone system, which consists of a molecular chaperone from the Hsc70 family, HscA in E. coli, and a co-chaperone of the J-domain family, Hsc20/HscB (known as Jac1 in fungi) [ 2 ]. The co-chaperone HscB recruits the scaffold protein for Fe-S cluster biogenesis Isu1/IscU, guiding it to the chaperone HscA [ 3 , 4 ], and enhances the intrinsic ATPase activity of the HscA [ 5 ].

1. Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p. EMBO J. 22, 4815-25
2. HscA and HscB stimulate [2Fe-2S] cluster transfer from IscU to apoferredoxin in an ATP-dependent reaction. Biochemistry 45, 11087-95
3. Characterization of the interaction between the J-protein Jac1p and the scaffold for Fe-S cluster biogenesis, Isu1p. J. Biol. Chem. 281, 14580-7
4. Interaction of J-protein co-chaperone Jac1 with Fe-S scaffold Isu is indispensable in vivo and conserved in evolution. J. Mol. Biol. 417, 1-12
5. Regulation of the HscA ATPase reaction cycle by the co-chaperone HscB and the iron-sulfur cluster assembly protein IscU. J. Biol. Chem. 279, 53924-31