Multiple mutations in polyketide synthase led to disruption of Psittacofulvin production across diverse parrot species
Abstract Polyketide synthases (PKSs) are crucial multidomain enzymes in diverse natural product biosynthesis. Parrots use a type I PKS to produce a unique pigment called psittacofulvin in their feathers. In domesticated budgerigars and lovebirds, the same amino acid substitution (R644W) within malon...
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Nature Portfolio
2025-01-01
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| Series: | Communications Biology |
| Online Access: | https://doi.org/10.1038/s42003-025-07537-7 |
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| author | Shatadru Ghosh Roy Jindřich Brejcha Petr Maršík Anna Bakhrat Moty Abdu Roberto Arbore Pedro Miguel Araújo Sandra Afonso Miguel Carneiro Iris Grossman-Haham Uri Abdu |
| author_facet | Shatadru Ghosh Roy Jindřich Brejcha Petr Maršík Anna Bakhrat Moty Abdu Roberto Arbore Pedro Miguel Araújo Sandra Afonso Miguel Carneiro Iris Grossman-Haham Uri Abdu |
| author_sort | Shatadru Ghosh Roy |
| collection | DOAJ |
| description | Abstract Polyketide synthases (PKSs) are crucial multidomain enzymes in diverse natural product biosynthesis. Parrots use a type I PKS to produce a unique pigment called psittacofulvin in their feathers. In domesticated budgerigars and lovebirds, the same amino acid substitution (R644W) within malonyl/acetyltransferase (MAT) domain of this enzyme has been shown to cause the blue phenotype with no psittacofulvin pigmentation, proposing a strong evolutionary constraint on the mechanism. Here, we identified seven previously unreported variants in PKS associated with defective psittacofulvin production in four diverse species, including three nonsense mutations. Intriguingly, three of the remaining nonsynonymous substitutions reside within the ketoacyl synthase (KS) domain, whereas one at MAT domain. The heterologous expression of these PKS variants in yeast confirmed complete or partial loss of psittacofulvin production. These findings establish PKS as a functionally conserved key-enzyme determining psittacofulvin-based hues among diverse parrots, highlighting multiple conserved domains essential for the PKS function. |
| format | Article |
| id | doaj-art-7d865e2010e447329c418fc6628aca51 |
| institution | Kabale University |
| issn | 2399-3642 |
| language | English |
| publishDate | 2025-01-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Communications Biology |
| spelling | doaj-art-7d865e2010e447329c418fc6628aca512025-01-19T12:35:36ZengNature PortfolioCommunications Biology2399-36422025-01-018111110.1038/s42003-025-07537-7Multiple mutations in polyketide synthase led to disruption of Psittacofulvin production across diverse parrot speciesShatadru Ghosh Roy0Jindřich Brejcha1Petr Maršík2Anna Bakhrat3Moty Abdu4Roberto Arbore5Pedro Miguel Araújo6Sandra Afonso7Miguel Carneiro8Iris Grossman-Haham9Uri Abdu10Department of Life Sciences, Ben-Gurion University of the NegevDepartment of Philosophy and History of Science, Faculty of Science, Charles UniversityDepartment of Food Science, Faculty of Agrobiology, Food, and Natural ResourcesDepartment of Life Sciences, Ben-Gurion University of the NegevST Lab Hashita 240CIBIO, Centro de Investigação em Biodiversidade e Recursos Genéticos, InBIO, Universidade do PortoCIBIO, Centro de Investigação em Biodiversidade e Recursos Genéticos, InBIO, Universidade do PortoCIBIO, Centro de Investigação em Biodiversidade e Recursos Genéticos, InBIO, Universidade do PortoCIBIO, Centro de Investigação em Biodiversidade e Recursos Genéticos, InBIO, Universidade do PortoDepartment of Life Sciences, Ben-Gurion University of the NegevDepartment of Life Sciences, Ben-Gurion University of the NegevAbstract Polyketide synthases (PKSs) are crucial multidomain enzymes in diverse natural product biosynthesis. Parrots use a type I PKS to produce a unique pigment called psittacofulvin in their feathers. In domesticated budgerigars and lovebirds, the same amino acid substitution (R644W) within malonyl/acetyltransferase (MAT) domain of this enzyme has been shown to cause the blue phenotype with no psittacofulvin pigmentation, proposing a strong evolutionary constraint on the mechanism. Here, we identified seven previously unreported variants in PKS associated with defective psittacofulvin production in four diverse species, including three nonsense mutations. Intriguingly, three of the remaining nonsynonymous substitutions reside within the ketoacyl synthase (KS) domain, whereas one at MAT domain. The heterologous expression of these PKS variants in yeast confirmed complete or partial loss of psittacofulvin production. These findings establish PKS as a functionally conserved key-enzyme determining psittacofulvin-based hues among diverse parrots, highlighting multiple conserved domains essential for the PKS function.https://doi.org/10.1038/s42003-025-07537-7 |
| spellingShingle | Shatadru Ghosh Roy Jindřich Brejcha Petr Maršík Anna Bakhrat Moty Abdu Roberto Arbore Pedro Miguel Araújo Sandra Afonso Miguel Carneiro Iris Grossman-Haham Uri Abdu Multiple mutations in polyketide synthase led to disruption of Psittacofulvin production across diverse parrot species Communications Biology |
| title | Multiple mutations in polyketide synthase led to disruption of Psittacofulvin production across diverse parrot species |
| title_full | Multiple mutations in polyketide synthase led to disruption of Psittacofulvin production across diverse parrot species |
| title_fullStr | Multiple mutations in polyketide synthase led to disruption of Psittacofulvin production across diverse parrot species |
| title_full_unstemmed | Multiple mutations in polyketide synthase led to disruption of Psittacofulvin production across diverse parrot species |
| title_short | Multiple mutations in polyketide synthase led to disruption of Psittacofulvin production across diverse parrot species |
| title_sort | multiple mutations in polyketide synthase led to disruption of psittacofulvin production across diverse parrot species |
| url | https://doi.org/10.1038/s42003-025-07537-7 |
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