Acquisition of new function through gene duplication in the metallocarboxypeptidase family
Abstract Gene duplication is a key first step in the process of expanding the functionality of a multigene family. In order to better understand the process of gene duplication and its role in the formation of new enzymes, we investigated recent duplication events in the M14 family of proteolytic en...
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2023-02-01
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| Series: | Scientific Reports |
| Online Access: | https://doi.org/10.1038/s41598-023-29800-9 |
| _version_ | 1797864796877488128 |
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| author | Daniel Fajardo Ritchie Saint Jean Peter J. Lyons |
| author_facet | Daniel Fajardo Ritchie Saint Jean Peter J. Lyons |
| author_sort | Daniel Fajardo |
| collection | DOAJ |
| description | Abstract Gene duplication is a key first step in the process of expanding the functionality of a multigene family. In order to better understand the process of gene duplication and its role in the formation of new enzymes, we investigated recent duplication events in the M14 family of proteolytic enzymes. Within vertebrates, four of 23 M14 genes were frequently found in duplicate form. While AEBP1, CPXM1, and CPZ genes were duplicated once through a large-scale, likely whole-genome duplication event, the CPO gene underwent many duplication events within fish and Xenopus lineages. Bioinformatic analyses of enzyme specificity and conservation suggested a greater amount of neofunctionalization and purifying selection in CPO paralogs compared with other CPA/B enzymes. To examine the functional consequences of evolutionary changes on CPO paralogs, the four CPO paralogs from Xenopus tropicalis were expressed in Sf9 and HEK293T cells. Immunocytochemistry showed subcellular distribution of Xenopus CPO paralogs to be similar to that of human CPO. Upon activation with trypsin, the enzymes demonstrated differential activity against three substrates, suggesting an acquisition of new function following duplication and subsequent mutagenesis. Characteristics such as gene size and enzyme activation mechanisms are possible contributors to the evolutionary capacity of the CPO gene. |
| first_indexed | 2024-04-09T22:58:31Z |
| format | Article |
| id | doaj.art-8435be84bb1f4c7195eb6adfe943f2e5 |
| institution | Directory Open Access Journal |
| issn | 2045-2322 |
| language | English |
| last_indexed | 2024-04-09T22:58:31Z |
| publishDate | 2023-02-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Scientific Reports |
| spelling | doaj.art-8435be84bb1f4c7195eb6adfe943f2e52023-03-22T11:08:28ZengNature PortfolioScientific Reports2045-23222023-02-0113111410.1038/s41598-023-29800-9Acquisition of new function through gene duplication in the metallocarboxypeptidase familyDaniel Fajardo0Ritchie Saint Jean1Peter J. Lyons2Department of Biology, Andrews UniversityDepartment of Biology, Andrews UniversityDepartment of Biology, Andrews UniversityAbstract Gene duplication is a key first step in the process of expanding the functionality of a multigene family. In order to better understand the process of gene duplication and its role in the formation of new enzymes, we investigated recent duplication events in the M14 family of proteolytic enzymes. Within vertebrates, four of 23 M14 genes were frequently found in duplicate form. While AEBP1, CPXM1, and CPZ genes were duplicated once through a large-scale, likely whole-genome duplication event, the CPO gene underwent many duplication events within fish and Xenopus lineages. Bioinformatic analyses of enzyme specificity and conservation suggested a greater amount of neofunctionalization and purifying selection in CPO paralogs compared with other CPA/B enzymes. To examine the functional consequences of evolutionary changes on CPO paralogs, the four CPO paralogs from Xenopus tropicalis were expressed in Sf9 and HEK293T cells. Immunocytochemistry showed subcellular distribution of Xenopus CPO paralogs to be similar to that of human CPO. Upon activation with trypsin, the enzymes demonstrated differential activity against three substrates, suggesting an acquisition of new function following duplication and subsequent mutagenesis. Characteristics such as gene size and enzyme activation mechanisms are possible contributors to the evolutionary capacity of the CPO gene.https://doi.org/10.1038/s41598-023-29800-9 |
| spellingShingle | Daniel Fajardo Ritchie Saint Jean Peter J. Lyons Acquisition of new function through gene duplication in the metallocarboxypeptidase family Scientific Reports |
| title | Acquisition of new function through gene duplication in the metallocarboxypeptidase family |
| title_full | Acquisition of new function through gene duplication in the metallocarboxypeptidase family |
| title_fullStr | Acquisition of new function through gene duplication in the metallocarboxypeptidase family |
| title_full_unstemmed | Acquisition of new function through gene duplication in the metallocarboxypeptidase family |
| title_short | Acquisition of new function through gene duplication in the metallocarboxypeptidase family |
| title_sort | acquisition of new function through gene duplication in the metallocarboxypeptidase family |
| url | https://doi.org/10.1038/s41598-023-29800-9 |
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