Abstract
Proline-specific peptidases (PSP) play a crucial role in the processing of fungal toxins, pheromones, and intracellular signaling. They are of particular interest to biotechnology, as they are able to hydrolyze proline-rich oligopeptides that give a bitter taste to food and can also cause an autoimmune celiac disease. We performed in silico analysis of PSP homologs in the genomes of 42 species of higher fungi which showed the presence of PSP homologs characteristic of various kingdoms of living organisms and belonging to different families of peptidases, including homologs of dipeptidyl peptidase 4 (DPP4) and prolyl aminopeptidase 1 found in almost all the studied fungal species. Homologs of proliniminopeptidases from the S33 family absent in humans were also found. Several studied homologs are characteristic of certain taxonomic groups of fungi. Phylogenetic analysis suggests a duplication of ancestral DPP4 into transmembrane and secreted versions, which predate the split of ascomycete and basidiomycete lineages. Comparative biochemical analysis of DPP4 in alkaliphilic and alkali-tolerant strains of fungi showed that, notwithstanding some individual features of these enzymes, in both cases, the studied DPP4 are active and stable under alkaline conditions and at high salt concentrations, which makes them viable candidates for biotechnology and bioengineering.
Highlights
Fungi occupy various ecological niches, owing to their remarkable physiological plasticity
10 different Proline-specific peptidases (PSP) were found in the species, including homologs of human APP1, cytosolic nonspecific dipeptidase (CND), dipeptidyl peptidase 4 (DPP4), leucine aminopeptidase (LAP), prolyl oligopeptidase (POP), and prolidase (XPD)
Homologs of DPP4 and APP1 were found in the genomes of almost all selected species, suggesting their important functional significance, while homologs of fibroblast activation protein (FAP), DPP6, DPP8, DPP9, DPP10, and
Summary
Fungi occupy various ecological niches, owing to their remarkable physiological plasticity. Several fungal species thrive in extreme temperatures and harsh radiation [1,2,3,4]. The extremophilic groups of fungi include fungi of alkaline habitats that can grow and develop at a pH of 10 or higher [5,6]. The survival of fungi depends on their ability to use nutrients from living or dead organic materials. The encoded set of enzymes largely determine the habitat these fungi can occupy. Differences in secreted enzymes can significantly affect their ability to colonize plants and animals. The peptidases secreted by fungi, performing trophic functions, cleave the bonds in protein substrates and lead to the formation of amino acids and peptides, which are absorbed by fungal cells and used in catabolic and biosynthetic processes
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