The conserved eukaryotic translation initiation factor 5A (eIF5A), which contains hypusine as a post-translational modification, plays a critical role in eukaryotic cell physiology. For instance, the deletion of the eif5A gene in Saccharomyces cerevisiae is lethal to cells. Besides, the inhibition of hypusination enzymes severely suppresses the ability of the cells to divide and halts the growth of mammalian cell populations. Therefore, the study of the structural features of eIF5A and its complexes with the enzymes deoxyhypusine synthase (DHS) and deoxyhypusine hydroxylase (DOHH) from the pathogenic yeast-like fungi Candida albicans, which catalyze the post-translational modification of eIF5A, will help in searching for new targets for the development of new antimycotics. This study presents an optimized protocol for the isolation and purification of the eIF5A protein from C. albicans and the structural analysis of this protein and its complex with the DHS enzyme by small-angle X-ray scattering.
Khanova et al. (Sun,) studied this question.