Systematic Analysis of the Lysine Succinylome in Candida albicans

Abstract

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.

Global analysis of lysine succinylome in the periodontal pathogen Porphyromonas gingivalis

“…Results from this study show that Ksuc sites are present in RagB, FimA (major subunit protein of the FimA fimbriae), Mfa1 (major subunit protein of the Mfa1 fimbriae), RgpA, RgpB, Kgp, and PorR (involved in A‐LPS biosynthesis). Given that Ksuc can change protein structure and function, the data from this study support the hypothesis that this modification is involved in the virulence of P gingivalis , similar to its role in other pathogenic bacteria or fungi …”

Systematic analysis of the lysine succinylome in the model medicinal mushroom Ganoderma lucidum

“…4b and Additional file 2: Table S4). These observations are consistent with the previous results in T. aestivum [7] and C. albicans [12]. Cellular component analysis revealed that succinylproteins were mainly distributed in cells (39.5%), macromolecular complexes (25.7%), organelles (24.5%) and membranes (7.5%) (Fig.…”

“…Therefore, proteins with K or R in corresponding sites are more easily to be the preferred substrates of lysine succinyltransferase in G. lucidum . It is noteworthy that the conserved motifs form strawberry stigmata [11], common wheat [7], C. albicans [12], and V. parahemolyticus [14] are different, indicating that different species contain unique succinylated proteins with specific functions.…”

“…In the past few years, lysine succinylation has been widely investigated at the level of proteomics thanks to the development of lysine-succinylated peptides immune precipitation technology. Succinylated proteins are found in large quantities in plants [7, 11], yeast [12], fungus [13], and bacteria [14–16]. These proteomic analyses revealed a wide range of roles for succinyl modification in various cellular functions such as catalytic activities, energy generation and photosynthesis in plants.…”

Al3+‐Morpholine‐appended Anthracene Ensemble as a Dual Photonic Switch for H2PO4− and CN− Ions and its Biological Applications

“…Image‐guided fluorogenic tracking of H 2 PO 4 − and CN − ions was demonstrated in Candida albicans (C.A), which are well‐known virulent primitive eukaryotic cells that typically resemble eukaryotic cells . Experiments were performed in C.A species considering the simplicity in culturing, cost effectiveness, and easier handling as compared to animal cells.…”