Abstract
The small ubiquitin-related modifier (SUMO) protein is an important component of the post-translational protein modification systems in eukaryotic cells. It is known to modify hundreds of proteins involved in diverse cellular processes, ranging from nuclear pore dynamics to signal transduction pathways. Owing to its reversible nature, the SUMO-conjugation of proteins (SUMOylation) holds a prominent place among mechanisms that regulate the functions of a wide array of cellular proteins. The dysfunctional SUMOylation system has been associated with many human diseases, including neurodegenerative and autoimmune disorders. Furthermore, the non-pathogenic yeast Saccharomyces cerevisiae has served as an excellent model to advance our understanding of enzymes involved in SUMOylation and proteins modified by SUMOylation. Taking advantage of the tools and knowledge obtained from the S. cerevisiae SUMOylation system, research on fungal SUMOylation is beginning to gather pace, and new insights into the role of SUMOylation in the pathobiology of medically important fungi are emerging. Here, we summarize the known information on components of the SUMOylation machinery, and consequences of overexpression or deletion of these components in the human pathogenic fungi, with major focus on two prevalent Candida bloodstream pathogens, C. albicans and C. glabrata. Additionally, we have identified SUMOylation components, through in silico analysis, in four medically relevant fungi, and compared their sequence similarity with S. cerevisiae counterparts. SUMOylation modulates the virulence of C. albicans and C. glabrata, while it is required for conidia production in Aspergillus nidulans and A. flavus. In addition to highlighting these recent developments, we discuss how SUMOylation fine tunes the expression of virulence factors, and influences survival of fungal cells under diverse stresses in vitro and in the mammalian host.
Highlights
A reversible post-translational modification of proteins, mediated by a highly conserved small ubiquitin-related modifier (SUMO), regulates numerous physiological processes [1,2,3]
The current review summarizes the key aspects of fungal SUMOylation systems and their role in fungal pathobiology
SUMO ligases contain the SP-RING domain which plays an important role in binding to Ubc9 directly [38,39]
Summary
A reversible post-translational modification of proteins, mediated by a highly conserved small ubiquitin-related modifier (SUMO), regulates numerous physiological processes [1,2,3]. ∼11 kDa polypeptide, that is attached covalently, via an isopeptide bond, to the amino group of the lysine residue in cellular substrate proteins [1,4] This conjugation is predominantly catalyzed by SUMO ligases, and is the fourth step in the process of SUMOylation [3,5]. E2-conjugating enzyme via a thioester linkage between the cysteine residue of the E2 enzyme and the the SUMO-GG motif; and (iv) E3 ligase-mediated formation of an isopeptide bond between the SUMO-GG motif; and (iv) E3 ligase-mediated formation of an isopeptide bond between the carboxyl carboxyl group of the C-terminal glycine of the SUMO protein and the ε-amino group of the specific group of the. Our aim is to provide an overview of fungal SUMOylation enzymes and SUMO-target proteins, and their functions in fungal physiology and virulence
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