Unraveling the Molecular Basis of Mycosporine Biosynthesis in Fungi
- Autores
- Sepúlveda, Dionisia; Campusano, Sebastián; Moliné, Martín; Barahona, Salvador; Baeza, Marcelo; Alcaíno, Jennifer; Colabella, Fernando; Urzúa, Blanca; Libkind, Diego; Cifuentes, Víctor
- Año de publicación
- 2023
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión aceptada
- Descripción
- The Phaffia rhodozyma UCD 67-385 genome harbors a 7873 bp cluster containing DDGS, OMT, and ATPG, encoding 2-desmethy-4-deoxygadusol synthase, O-methyl transferase, and ATP- grasp ligase, respectively, of the mycosporine glutaminol (MG) biosynthesis pathway. Homozy- gous deletion mutants of the entire cluster, single-gene mutants, and the ∆ddgs−/−;∆omt−/− and ∆omt−/−;∆atpg−/− double-gene mutants did not produce mycosporines. However, ∆atpg−/− accu- mulated the intermediate 4-deoxygadusol. Heterologous expression of the DDGS and OMT or DDGS, OMT, and ATPG cDNAs in Saccharomyces cerevisiae led to 4-deoxygadusol or MG production, respec- tively. Genetic integration of the complete cluster into the genome of the non-mycosporine-producing CBS 6938 wild-type strain resulted in a transgenic strain (CBS 6938_MYC) that produced MG and my- cosporine glutaminol glucoside. These results indicate the function of DDGS, OMT, and ATPG in the mycosporine biosynthesis pathway. The transcription factor gene mutants ∆mig1−/−, ∆cyc8−/−, and ∆opi1−/− showed upregulation, ∆rox1−/− and ∆skn7−/− showed downregulation, and ∆tup6−/− and ∆yap6−/− showed no effect on mycosporinogenesis in glucose-containing medium. Finally, comparative analysis of the cluster sequences in several P. rhodozyma strains and the four newly described species of the genus showed the phylogenetic relationship of the P. rhodozyma strains and their differentiation from the other species of the genus Phaffia.
Fil: Sepúlveda, Dionisia. Universidad de Chile. Facultad de Ciencias. Departamento de Ciencias Ecológicas; Chile.
Fil: Campusano, Sebastián. Universidad de Chile. Facultad de Ciencias. Departamento de Ciencias Ecológicas; Chile.
Fil: Moliné, Martín. Universidad Nacional del Comahue. Centro Regional Universitario Bariloche; Argentina.
Fil: Moliné, Martín. Universidad Nacional del Comahue. Instituto de Investigaciones en Biodiversidad y Medioambiente; Argentina.
Fil: Moliné, Martín. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina.
Fil: Barahona, Salvador. Universidad de Chile. Facultad de Ciencias. Departamento de Ciencias Ecológicas; Chile.
Fil: Baeza, Marcelo. Universidad de Chile. Facultad de Ciencias. Departamento de Ciencias Ecológicas; Chile.
Fil: Alcaíno, Jennifer. Universidad de Chile. Facultad de Ciencias. Departamento de Ciencias Ecológicas; Chile.
Fil: Colabella, Fernando. Independent Researcher Bariloche; Argentina.
Fil: Urzúa, Blanca. Universidad de Chile. Facultad de Odontología. Instituto de Investigación en Ciencias Odontológicas; Chile.
Fil: Libkind, Diego. Universidad Nacional del Comahue. Centro Regional Universitario Bariloche; Argentina.
Fil: Libkind, Diego. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina.
Fil: Cifuentes, Víctor. Universidad de Chile. Facultad de Ciencias. Departamento de Ciencias Ecológicas; Chile. - Fuente
- International Journal of Molecular Sciences. 2023, 24, 5930
- Materia
-
Phaffia
Mycosporine
Genes cluster
Secondary metabolite
Ciencias de la Tierra y Medio Ambiente
Ciencias Biomédicas - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
.jpg)
- Institución
- Universidad Nacional del Comahue
- OAI Identificador
- oai:rdi.uncoma.edu.ar:uncomaid/17451
Ver los metadatos del registro completo
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Unraveling the Molecular Basis of Mycosporine Biosynthesis in FungiSepúlveda, DionisiaCampusano, SebastiánMoliné, MartínBarahona, SalvadorBaeza, MarceloAlcaíno, JenniferColabella, FernandoUrzúa, BlancaLibkind, DiegoCifuentes, VíctorPhaffiaMycosporineGenes clusterSecondary metaboliteCiencias de la Tierra y Medio AmbienteCiencias BiomédicasThe Phaffia rhodozyma UCD 67-385 genome harbors a 7873 bp cluster containing DDGS, OMT, and ATPG, encoding 2-desmethy-4-deoxygadusol synthase, O-methyl transferase, and ATP- grasp ligase, respectively, of the mycosporine glutaminol (MG) biosynthesis pathway. Homozy- gous deletion mutants of the entire cluster, single-gene mutants, and the ∆ddgs−/−;∆omt−/− and ∆omt−/−;∆atpg−/− double-gene mutants did not produce mycosporines. However, ∆atpg−/− accu- mulated the intermediate 4-deoxygadusol. Heterologous expression of the DDGS and OMT or DDGS, OMT, and ATPG cDNAs in Saccharomyces cerevisiae led to 4-deoxygadusol or MG production, respec- tively. Genetic integration of the complete cluster into the genome of the non-mycosporine-producing CBS 6938 wild-type strain resulted in a transgenic strain (CBS 6938_MYC) that produced MG and my- cosporine glutaminol glucoside. These results indicate the function of DDGS, OMT, and ATPG in the mycosporine biosynthesis pathway. The transcription factor gene mutants ∆mig1−/−, ∆cyc8−/−, and ∆opi1−/− showed upregulation, ∆rox1−/− and ∆skn7−/− showed downregulation, and ∆tup6−/− and ∆yap6−/− showed no effect on mycosporinogenesis in glucose-containing medium. Finally, comparative analysis of the cluster sequences in several P. rhodozyma strains and the four newly described species of the genus showed the phylogenetic relationship of the P. rhodozyma strains and their differentiation from the other species of the genus Phaffia.Fil: Sepúlveda, Dionisia. Universidad de Chile. Facultad de Ciencias. Departamento de Ciencias Ecológicas; Chile.Fil: Campusano, Sebastián. Universidad de Chile. Facultad de Ciencias. Departamento de Ciencias Ecológicas; Chile.Fil: Moliné, Martín. Universidad Nacional del Comahue. Centro Regional Universitario Bariloche; Argentina.Fil: Moliné, Martín. Universidad Nacional del Comahue. Instituto de Investigaciones en Biodiversidad y Medioambiente; Argentina.Fil: Moliné, Martín. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina.Fil: Barahona, Salvador. Universidad de Chile. Facultad de Ciencias. Departamento de Ciencias Ecológicas; Chile.Fil: Baeza, Marcelo. Universidad de Chile. Facultad de Ciencias. Departamento de Ciencias Ecológicas; Chile.Fil: Alcaíno, Jennifer. Universidad de Chile. Facultad de Ciencias. Departamento de Ciencias Ecológicas; Chile.Fil: Colabella, Fernando. Independent Researcher Bariloche; Argentina.Fil: Urzúa, Blanca. Universidad de Chile. Facultad de Odontología. Instituto de Investigación en Ciencias Odontológicas; Chile.Fil: Libkind, Diego. Universidad Nacional del Comahue. Centro Regional Universitario Bariloche; Argentina.Fil: Libkind, Diego. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina.Fil: Cifuentes, Víctor. Universidad de Chile. Facultad de Ciencias. Departamento de Ciencias Ecológicas; Chile.MDPI2023info:eu-repo/semantics/articleinfo:eu-repo/semantics/acceptedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfpp. 1-19application/pdfhttp://rdi.uncoma.edu.ar/handle/uncomaid/17451International Journal of Molecular Sciences. 2023, 24, 5930reponame:Repositorio Digital Institucional (UNCo)instname:Universidad Nacional del Comahueenghttps://doi.org/10.3390/ijms24065930info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/2025-10-16T10:05:45Zoai:rdi.uncoma.edu.ar:uncomaid/17451instacron:UNCoInstitucionalhttp://rdi.uncoma.edu.ar/Universidad públicaNo correspondehttp://rdi.uncoma.edu.ar/oaimirtha.mateo@biblioteca.uncoma.edu.ar; adriana.acuna@biblioteca.uncoma.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:71082025-10-16 10:05:45.429Repositorio Digital Institucional (UNCo) - Universidad Nacional del Comahuefalse |
| dc.title.none.fl_str_mv |
Unraveling the Molecular Basis of Mycosporine Biosynthesis in Fungi |
| title |
Unraveling the Molecular Basis of Mycosporine Biosynthesis in Fungi |
| spellingShingle |
Unraveling the Molecular Basis of Mycosporine Biosynthesis in Fungi Sepúlveda, Dionisia Phaffia Mycosporine Genes cluster Secondary metabolite Ciencias de la Tierra y Medio Ambiente Ciencias Biomédicas |
| title_short |
Unraveling the Molecular Basis of Mycosporine Biosynthesis in Fungi |
| title_full |
Unraveling the Molecular Basis of Mycosporine Biosynthesis in Fungi |
| title_fullStr |
Unraveling the Molecular Basis of Mycosporine Biosynthesis in Fungi |
| title_full_unstemmed |
Unraveling the Molecular Basis of Mycosporine Biosynthesis in Fungi |
| title_sort |
Unraveling the Molecular Basis of Mycosporine Biosynthesis in Fungi |
| dc.creator.none.fl_str_mv |
Sepúlveda, Dionisia Campusano, Sebastián Moliné, Martín Barahona, Salvador Baeza, Marcelo Alcaíno, Jennifer Colabella, Fernando Urzúa, Blanca Libkind, Diego Cifuentes, Víctor |
| author |
Sepúlveda, Dionisia |
| author_facet |
Sepúlveda, Dionisia Campusano, Sebastián Moliné, Martín Barahona, Salvador Baeza, Marcelo Alcaíno, Jennifer Colabella, Fernando Urzúa, Blanca Libkind, Diego Cifuentes, Víctor |
| author_role |
author |
| author2 |
Campusano, Sebastián Moliné, Martín Barahona, Salvador Baeza, Marcelo Alcaíno, Jennifer Colabella, Fernando Urzúa, Blanca Libkind, Diego Cifuentes, Víctor |
| author2_role |
author author author author author author author author author |
| dc.subject.none.fl_str_mv |
Phaffia Mycosporine Genes cluster Secondary metabolite Ciencias de la Tierra y Medio Ambiente Ciencias Biomédicas |
| topic |
Phaffia Mycosporine Genes cluster Secondary metabolite Ciencias de la Tierra y Medio Ambiente Ciencias Biomédicas |
| dc.description.none.fl_txt_mv |
The Phaffia rhodozyma UCD 67-385 genome harbors a 7873 bp cluster containing DDGS, OMT, and ATPG, encoding 2-desmethy-4-deoxygadusol synthase, O-methyl transferase, and ATP- grasp ligase, respectively, of the mycosporine glutaminol (MG) biosynthesis pathway. Homozy- gous deletion mutants of the entire cluster, single-gene mutants, and the ∆ddgs−/−;∆omt−/− and ∆omt−/−;∆atpg−/− double-gene mutants did not produce mycosporines. However, ∆atpg−/− accu- mulated the intermediate 4-deoxygadusol. Heterologous expression of the DDGS and OMT or DDGS, OMT, and ATPG cDNAs in Saccharomyces cerevisiae led to 4-deoxygadusol or MG production, respec- tively. Genetic integration of the complete cluster into the genome of the non-mycosporine-producing CBS 6938 wild-type strain resulted in a transgenic strain (CBS 6938_MYC) that produced MG and my- cosporine glutaminol glucoside. These results indicate the function of DDGS, OMT, and ATPG in the mycosporine biosynthesis pathway. The transcription factor gene mutants ∆mig1−/−, ∆cyc8−/−, and ∆opi1−/− showed upregulation, ∆rox1−/− and ∆skn7−/− showed downregulation, and ∆tup6−/− and ∆yap6−/− showed no effect on mycosporinogenesis in glucose-containing medium. Finally, comparative analysis of the cluster sequences in several P. rhodozyma strains and the four newly described species of the genus showed the phylogenetic relationship of the P. rhodozyma strains and their differentiation from the other species of the genus Phaffia. Fil: Sepúlveda, Dionisia. Universidad de Chile. Facultad de Ciencias. Departamento de Ciencias Ecológicas; Chile. Fil: Campusano, Sebastián. Universidad de Chile. Facultad de Ciencias. Departamento de Ciencias Ecológicas; Chile. Fil: Moliné, Martín. Universidad Nacional del Comahue. Centro Regional Universitario Bariloche; Argentina. Fil: Moliné, Martín. Universidad Nacional del Comahue. Instituto de Investigaciones en Biodiversidad y Medioambiente; Argentina. Fil: Moliné, Martín. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Fil: Barahona, Salvador. Universidad de Chile. Facultad de Ciencias. Departamento de Ciencias Ecológicas; Chile. Fil: Baeza, Marcelo. Universidad de Chile. Facultad de Ciencias. Departamento de Ciencias Ecológicas; Chile. Fil: Alcaíno, Jennifer. Universidad de Chile. Facultad de Ciencias. Departamento de Ciencias Ecológicas; Chile. Fil: Colabella, Fernando. Independent Researcher Bariloche; Argentina. Fil: Urzúa, Blanca. Universidad de Chile. Facultad de Odontología. Instituto de Investigación en Ciencias Odontológicas; Chile. Fil: Libkind, Diego. Universidad Nacional del Comahue. Centro Regional Universitario Bariloche; Argentina. Fil: Libkind, Diego. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Fil: Cifuentes, Víctor. Universidad de Chile. Facultad de Ciencias. Departamento de Ciencias Ecológicas; Chile. |
| description |
The Phaffia rhodozyma UCD 67-385 genome harbors a 7873 bp cluster containing DDGS, OMT, and ATPG, encoding 2-desmethy-4-deoxygadusol synthase, O-methyl transferase, and ATP- grasp ligase, respectively, of the mycosporine glutaminol (MG) biosynthesis pathway. Homozy- gous deletion mutants of the entire cluster, single-gene mutants, and the ∆ddgs−/−;∆omt−/− and ∆omt−/−;∆atpg−/− double-gene mutants did not produce mycosporines. However, ∆atpg−/− accu- mulated the intermediate 4-deoxygadusol. Heterologous expression of the DDGS and OMT or DDGS, OMT, and ATPG cDNAs in Saccharomyces cerevisiae led to 4-deoxygadusol or MG production, respec- tively. Genetic integration of the complete cluster into the genome of the non-mycosporine-producing CBS 6938 wild-type strain resulted in a transgenic strain (CBS 6938_MYC) that produced MG and my- cosporine glutaminol glucoside. These results indicate the function of DDGS, OMT, and ATPG in the mycosporine biosynthesis pathway. The transcription factor gene mutants ∆mig1−/−, ∆cyc8−/−, and ∆opi1−/− showed upregulation, ∆rox1−/− and ∆skn7−/− showed downregulation, and ∆tup6−/− and ∆yap6−/− showed no effect on mycosporinogenesis in glucose-containing medium. Finally, comparative analysis of the cluster sequences in several P. rhodozyma strains and the four newly described species of the genus showed the phylogenetic relationship of the P. rhodozyma strains and their differentiation from the other species of the genus Phaffia. |
| publishDate |
2023 |
| dc.date.none.fl_str_mv |
2023 |
| dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/acceptedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
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article |
| status_str |
acceptedVersion |
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http://rdi.uncoma.edu.ar/handle/uncomaid/17451 |
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http://rdi.uncoma.edu.ar/handle/uncomaid/17451 |
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eng |
| language |
eng |
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https://doi.org/10.3390/ijms24065930 |
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info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
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openAccess |
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https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
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application/pdf pp. 1-19 application/pdf |
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MDPI |
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MDPI |
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International Journal of Molecular Sciences. 2023, 24, 5930 reponame:Repositorio Digital Institucional (UNCo) instname:Universidad Nacional del Comahue |
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Universidad Nacional del Comahue |
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Repositorio Digital Institucional (UNCo) - Universidad Nacional del Comahue |
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mirtha.mateo@biblioteca.uncoma.edu.ar; adriana.acuna@biblioteca.uncoma.edu.ar |
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