This Recombinant Shigella flexneri grxD protein was made through genetic engineering. By putting the grxD gene into the genetic material of E.coli cell, the E.coli could be used as factories or producers to make the desired grxD protein for research uses. The expression region of this protein is at 1-115aa. N-terminal 6xHis-SUMO tag was used in the expression process. The purity is 85%+ determined by SDS-PAGE.

The cytosolic monothiol glutaredoxin GrxD plays a role in adaptation to iron starvation during infection. GrxD is repressed by the transcription factor SreA in iron replete conditions. During iron starvation, GrxD displays predominant nuclear localization. Downregulation of GrxD expression results in de-repression of genes involved in iron-dependent pathways and repression of genes involved in iron acquisition during iron starvation, but did not significantly affect these genes during iron sufficiency. GrxD displays protein-protein interaction with components of the cytosolic iron-sulfur cluster biosynthetic machinery, indicating a role in this process, and with the transcription factors SreA and HapX, which mediate iron regulation of iron acquisition and iron-dependent pathways. There is a GrxD-independent mechanism for sensing iron sufficiency by HapX. Inactivation of SreA suppresses the lethal effect caused by GrxD inactivation. Taken together, this study demonstrates that GrxD is crucial for iron homeostasis in A. fumigatus.