THE ROLE OF THE THREE GLRX3 DOMAINS IN THE MATURATION OF CYTOSOLIC FE-S PROTEINS

This study investigates the role of the multidomain protein GLRX3 in the cytosolic iron–sulfur cluster assembly (CIA) pathway, focusing on its function in [4Fe-4S] cluster maturation on NUBP1. GLRX3, which forms a [2Fe-2S]-bridged homodimer, can transfer [2Fe-2S] clusters and lead to the assembly of a [4Fe-4S] cluster on NUBP1 in vitro through a reductive coupling process. To elucidate the specific contribution of the three GLRX3 domains in this mechanism, different protein constructs and mutants were generated and characterized using UV-Vis, NMR spectroscopy, and size-exclusion chromatography.