<i>Aspergillus fumigatus</i> Metallothionein CmtA Binds and Receives a [2Fe-2S] Cluster from Monothiol Glutaredoxin GrxD.

ABSTRACT: Iron homeostasis is essential for the virulence of the opportunistic fungal pathogen Aspergillus fumigatus. The cytosolic monothiol glutaredoxin GrxD was recently shown to play a critical role in A. fumigatus iron metabolism via regulation of iron-sulfur (Fe-S) binding iron-responsive transcription factors and interaction with components of the cytosolic Fe-S cluster assembly pathway. Interestingly, the putative copper-binding metallothionein CmtA was also identified as a binding partner for GrxD; however, the metal-binding properties of both proteins and the nature of their interactions were unclear. Here, we addressed these open questions by recombinant expression and purification of GrxD and CmtA and analysis of their metal-protein and protein-protein interactions. Using e

SUBMITTER: Eap D 

PROVIDER: S-EPMC12716842 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature