Abstract
Fanconi Anemia Complementation J protein (FANCJ) belongs to SF2 helicases superfamily and proper function of FANCJ is crucial for disease regulation and control, as most of these mutations are related to maladies. As other SF2 helicases, FANCJ has a conserved domain containing four cysteine residues, which is the binding site of the iron-sulfur ([Fe-S]) cluster, an essential cofactor for life activities. However, the role of the [Fe-S] cluster is currently unclear. Thus, the ability of the FANCJ to coordinate an iron-sulfur ([Fe-S]) cluster is likely associated with the appropriate function of cells and the manifestation of diseases. In this work, I focused on FANCJ-TR1, a truncated version of FANCJ and is used to explore how the physical and chemical property of [Fe- S] cluster is perturbed by mutation samples. I also constructed three clinical mutants, G304E, H317Y, and A349P based on FANCJ-TR1 with a solubility enhancement tag (SET), MBP. The aim of this work is to compare the differences of the [Fe-S] cluster harbored by FANCJ-TR1 and the three mutants, and therefore give us a hint of the relationship between the assembly and properties of the [Fe-S] cluster and disorder behaviors caused by defective FANCJ.