Systematic Analysis of the Lysine Succinylome in Candida albicans

Candida albicans is the most common human fungal
pathogen for both immunocompetent and immunocompromised individuals.
Lysine succinylation is a frequently occurring post-translational
modification that is found in many organisms; however, the role of
succinylation is still under investigation. Here, we initiated a first
screening of lysine succinylation in C. albicans. We identified 1550 succinylation sites from 389 proteins in C. albicans, demonstrating that succinylation is
conservative in this organism. However, the lysine succinylation sites
showed some difference in C. albicans, with the overlapping rates between C. albicans and other species ranging from 55% for Saccharomyces
cerevisiae, 40% for human, 35% for mouse, and to only
16% for Escherichia coli. The further
bioinformatics analysis indicated that the succinylated proteins were
involved in a wide range of cellular functions with diverse subcellular
localizations. Furthermore, we discovered that lysine succinylation
could coexist with phosphorylation and/or acetylation in C. albicans. The KEGG enrichment pathway analysis
of these succinylated proteins suggested that succinylation may play
an indispensable role in the regulation of the tricarboxylic acid
cycle. The bioinformatic data obtained from this study therefore enable
the depth-resolved physiological roles of lysine succinylation in C. albicans.