Origins and Evolution of the α-L-Fucosidases: From Bacteria to Metazoans
α-L-fucosidases (EC 3.2.1.51, FUC), belonging to the glycoside hydrolase family 29 (GH29), play important roles in several biological processes and are markers used for detecting hepatocellular carcinoma. In this study, a protein sequence similarity network (SSN) was generated and a subsequent evolu...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2019-08-01
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| Series: | Frontiers in Microbiology |
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| Online Access: | https://www.frontiersin.org/article/10.3389/fmicb.2019.01756/full |
| _version_ | 1818540127631179776 |
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| author | Jia You Shujin Lin Tao Jiang |
| author_facet | Jia You Shujin Lin Tao Jiang |
| author_sort | Jia You |
| collection | DOAJ |
| description | α-L-fucosidases (EC 3.2.1.51, FUC), belonging to the glycoside hydrolase family 29 (GH29), play important roles in several biological processes and are markers used for detecting hepatocellular carcinoma. In this study, a protein sequence similarity network (SSN) was generated and a subsequent evolutionary analysis was performed to understand the enzymes comprehensively. The SSN indicated that the proteins in the FUC family are mainly present in bacteria, fungi, metazoans, plants, as well as in archaea, but less abundantly. The sequences in bacteria were found to be more diverse than those in other taxonomic groups. The SSN and a phylogenetic tree both supported that the proteins in the FUC family can be classified into 3 subfamilies. FUCs in each subfamily are under the pressure of negative selection. The enzymes from metazoans, fungi, and plants separated into the three subfamilies and shared high similarity with the bacterial homologs. The multiple sequence alignment results indicated that the amino acid residues for binding α-L-fucosidase and catalysis are highly conserved in the 3 subfamilies; however, the evolutionary patterns were different, based on the coevolution analysis in the subfamily of metazoans and bacteria. Finally, gene duplication plays an important role for α-L-fucosidase evolution, not only in metazoans, but also in bacteria and fungi. |
| first_indexed | 2024-12-11T21:51:12Z |
| format | Article |
| id | doaj.art-52d3c050bf344fd59444f75749a9424b |
| institution | Directory Open Access Journal |
| issn | 1664-302X |
| language | English |
| last_indexed | 2024-12-11T21:51:12Z |
| publishDate | 2019-08-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Microbiology |
| spelling | doaj.art-52d3c050bf344fd59444f75749a9424b2022-12-22T00:49:28ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2019-08-011010.3389/fmicb.2019.01756466379Origins and Evolution of the α-L-Fucosidases: From Bacteria to MetazoansJia You0Shujin Lin1Tao Jiang2Department of Hepatology, The Liver Center, The First Affiliated Hospital of Fujian Medical University, Fuzhou, ChinaCollege of Biological Science and Engineering, Fuzhou University, Fuzhou, ChinaDepartment of Urology, The First Affiliated Hospital of Fujian Medical University, Fuzhou, Chinaα-L-fucosidases (EC 3.2.1.51, FUC), belonging to the glycoside hydrolase family 29 (GH29), play important roles in several biological processes and are markers used for detecting hepatocellular carcinoma. In this study, a protein sequence similarity network (SSN) was generated and a subsequent evolutionary analysis was performed to understand the enzymes comprehensively. The SSN indicated that the proteins in the FUC family are mainly present in bacteria, fungi, metazoans, plants, as well as in archaea, but less abundantly. The sequences in bacteria were found to be more diverse than those in other taxonomic groups. The SSN and a phylogenetic tree both supported that the proteins in the FUC family can be classified into 3 subfamilies. FUCs in each subfamily are under the pressure of negative selection. The enzymes from metazoans, fungi, and plants separated into the three subfamilies and shared high similarity with the bacterial homologs. The multiple sequence alignment results indicated that the amino acid residues for binding α-L-fucosidase and catalysis are highly conserved in the 3 subfamilies; however, the evolutionary patterns were different, based on the coevolution analysis in the subfamily of metazoans and bacteria. Finally, gene duplication plays an important role for α-L-fucosidase evolution, not only in metazoans, but also in bacteria and fungi.https://www.frontiersin.org/article/10.3389/fmicb.2019.01756/fullα-L-fucosidaseevolutionsequence similarity networkbacteriametazoa |
| spellingShingle | Jia You Shujin Lin Tao Jiang Origins and Evolution of the α-L-Fucosidases: From Bacteria to Metazoans Frontiers in Microbiology α-L-fucosidase evolution sequence similarity network bacteria metazoa |
| title | Origins and Evolution of the α-L-Fucosidases: From Bacteria to Metazoans |
| title_full | Origins and Evolution of the α-L-Fucosidases: From Bacteria to Metazoans |
| title_fullStr | Origins and Evolution of the α-L-Fucosidases: From Bacteria to Metazoans |
| title_full_unstemmed | Origins and Evolution of the α-L-Fucosidases: From Bacteria to Metazoans |
| title_short | Origins and Evolution of the α-L-Fucosidases: From Bacteria to Metazoans |
| title_sort | origins and evolution of the α l fucosidases from bacteria to metazoans |
| topic | α-L-fucosidase evolution sequence similarity network bacteria metazoa |
| url | https://www.frontiersin.org/article/10.3389/fmicb.2019.01756/full |
| work_keys_str_mv | AT jiayou originsandevolutionofthealfucosidasesfrombacteriatometazoans AT shujinlin originsandevolutionofthealfucosidasesfrombacteriatometazoans AT taojiang originsandevolutionofthealfucosidasesfrombacteriatometazoans |