This study investigates the role of human GLRX3 in cytosolic iron–sulfur cluster assembly, focusing on its ability to transfer [2Fe-2S] clusters to NUBP1, a scaffold protein for [4Fe-4S] maturation. By generating domain-specific constructs and mutants of GLRX3 and analyzing them with biochemical and spectroscopic methods (UV-Vis, NMR, SEC), we found that the GrxA and GrxB domains act cooperatively to assemble a [4Fe-4S] cluster on NUBP1, while the Trx domain is not required for this activity.
Unraveling the function of GLRX3 domains in the maturation of human cytosolic Fe-S proteins / Rosanna Cuccaro, Francesca Camponeschi, Lucia Banci. - ELETTRONICO. - (2025), pp. 1-1. ( "Peptide and Protein Metalation").
Unraveling the function of GLRX3 domains in the maturation of human cytosolic Fe-S proteins
Rosanna Cuccaro;Francesca Camponeschi;Lucia Banci
2025
Abstract
This study investigates the role of human GLRX3 in cytosolic iron–sulfur cluster assembly, focusing on its ability to transfer [2Fe-2S] clusters to NUBP1, a scaffold protein for [4Fe-4S] maturation. By generating domain-specific constructs and mutants of GLRX3 and analyzing them with biochemical and spectroscopic methods (UV-Vis, NMR, SEC), we found that the GrxA and GrxB domains act cooperatively to assemble a [4Fe-4S] cluster on NUBP1, while the Trx domain is not required for this activity.
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