Proline-Specific Fungal Peptidases: Genomic Analysis and Identification of Secreted DPP4 in Alkaliphilic and Alkalitolerant Fungi
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 autoimm...
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| Format: | Article |
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MDPI AG
2021-09-01
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| Series: | Journal of Fungi |
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| Online Access: | https://www.mdpi.com/2309-608X/7/9/744 |
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| author | Nikita Alkin Yakov Dunaevsky Elena Elpidina Galina Beljakova Valeria Tereshchenkova Irina Filippova Mikhail Belozersky |
| author_facet | Nikita Alkin Yakov Dunaevsky Elena Elpidina Galina Beljakova Valeria Tereshchenkova Irina Filippova Mikhail Belozersky |
| author_sort | Nikita Alkin |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-10T07:32:24Z |
| format | Article |
| id | doaj.art-e466e9074a6d4d4197b3f871726e215a |
| institution | Directory Open Access Journal |
| issn | 2309-608X |
| language | English |
| last_indexed | 2024-03-10T07:32:24Z |
| publishDate | 2021-09-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Journal of Fungi |
| spelling | doaj.art-e466e9074a6d4d4197b3f871726e215a2023-11-22T13:48:18ZengMDPI AGJournal of Fungi2309-608X2021-09-017974410.3390/jof7090744Proline-Specific Fungal Peptidases: Genomic Analysis and Identification of Secreted DPP4 in Alkaliphilic and Alkalitolerant FungiNikita Alkin0Yakov Dunaevsky1Elena Elpidina2Galina Beljakova3Valeria Tereshchenkova4Irina Filippova5Mikhail Belozersky6Biological Faculty, Lomonosov Moscow State University, 119991 Moscow, RussiaA.N. Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119991 Moscow, RussiaA.N. Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119991 Moscow, RussiaBiological Faculty, Lomonosov Moscow State University, 119991 Moscow, RussiaChemical Faculty, Lomonosov Moscow State University, 119991 Moscow, RussiaChemical Faculty, Lomonosov Moscow State University, 119991 Moscow, RussiaA.N. Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119991 Moscow, RussiaProline-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.https://www.mdpi.com/2309-608X/7/9/744ascomycetesalkaliphilic and alkali-tolerant fungibasidiomycetesbioinformatic analysisproline-specific peptidasessecretion |
| spellingShingle | Nikita Alkin Yakov Dunaevsky Elena Elpidina Galina Beljakova Valeria Tereshchenkova Irina Filippova Mikhail Belozersky Proline-Specific Fungal Peptidases: Genomic Analysis and Identification of Secreted DPP4 in Alkaliphilic and Alkalitolerant Fungi Journal of Fungi ascomycetes alkaliphilic and alkali-tolerant fungi basidiomycetes bioinformatic analysis proline-specific peptidases secretion |
| title | Proline-Specific Fungal Peptidases: Genomic Analysis and Identification of Secreted DPP4 in Alkaliphilic and Alkalitolerant Fungi |
| title_full | Proline-Specific Fungal Peptidases: Genomic Analysis and Identification of Secreted DPP4 in Alkaliphilic and Alkalitolerant Fungi |
| title_fullStr | Proline-Specific Fungal Peptidases: Genomic Analysis and Identification of Secreted DPP4 in Alkaliphilic and Alkalitolerant Fungi |
| title_full_unstemmed | Proline-Specific Fungal Peptidases: Genomic Analysis and Identification of Secreted DPP4 in Alkaliphilic and Alkalitolerant Fungi |
| title_short | Proline-Specific Fungal Peptidases: Genomic Analysis and Identification of Secreted DPP4 in Alkaliphilic and Alkalitolerant Fungi |
| title_sort | proline specific fungal peptidases genomic analysis and identification of secreted dpp4 in alkaliphilic and alkalitolerant fungi |
| topic | ascomycetes alkaliphilic and alkali-tolerant fungi basidiomycetes bioinformatic analysis proline-specific peptidases secretion |
| url | https://www.mdpi.com/2309-608X/7/9/744 |
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