Diversification of substrate specificities in teleostei Fads2: characterization of Δ4 and Δ6Δ5 desaturases of Chirostoma estor

Currently existing data show that the capability for long-chain PUFA (LC-PUFA) biosynthesis in teleost fi sh is more diverse than in other vertebrates. Such diversity has been primarily linked to the subfunctionalization that teleostei fatty acyl desaturase (Fads)2 desaturases have undergone during...

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Autores: Fonseca-Madrigal, Jorge, Navarro, Juan Carlos, Hontoria, Francisco, Tocher, Douglas R., Martínez-Palacios, Carlos A., Monroig, Óscar
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2014
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/144098
Acceso en línea:http://hdl.handle.net/10261/144098
Access Level:acceso abierto
Palabra clave:Evolution
Fatty acyl desaturase 2
Long-chain polyunsaturated fatty acids
Teleosts
Elongase of very long-chain fatty acids
Biosynthesis
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spelling Diversification of substrate specificities in teleostei Fads2: characterization of Δ4 and Δ6Δ5 desaturases of Chirostoma estorFonseca-Madrigal, JorgeNavarro, Juan CarlosHontoria, FranciscoTocher, Douglas R.Martínez-Palacios, Carlos A.Monroig, ÓscarEvolutionFatty acyl desaturase 2Long-chain polyunsaturated fatty acidsTeleostsElongase of very long-chain fatty acidsBiosynthesisCurrently existing data show that the capability for long-chain PUFA (LC-PUFA) biosynthesis in teleost fi sh is more diverse than in other vertebrates. Such diversity has been primarily linked to the subfunctionalization that teleostei fatty acyl desaturase (Fads)2 desaturases have undergone during evolution. We previously showed that Chirostoma estor , one of the few representatives of freshwater atherinopsids, had the ability for LC-PUFA biosynthesis from C 18 PUFA precursors, in agreement with this species having unusually high contents of DHA. The particular ancestry and pattern of LC-PUFA biosynthesis activity of C. estor make this species an excellent model for study to gain further insight into LC-PUFA biosynthetic abilities among teleosts. The present study aimed to characterize cDNA sequences encoding fatty acyl elongases and desaturases, key genes involved in the LC-PUFA biosynthesis. Results show that C. estor expresses an elongase of very long-chain FA (Elovl)5 elongase and two Fads2 desaturases displaying 4 and 6/5 specifi cities, thus allowing us to conclude that these three genes cover all the enzymatic abilities required for LC-PUFA biosynthesis from C 18 PUFA. In addition, the specifi cities of the C. estor Fads2 enabled us to propose potential evolutionary patterns and mechanisms for subfunctionalization of Fads2 among fi sh lineages. -Fonseca- Madrigal, J., J. C. Navarro, F. Hontoria, D. R. Tocher, C. A. Martínez-Palacios, and Ó. Monroig. Diversifi cation of substrate specifi cities in teleostei Fads2: characterization of 4 and 6 5 desaturases of Chirostoma estor . J. Lipid Res. 2014. 55: 1408 - 1419. © 2014 by the American Society for Biochemistry and Molecular Biology, Inc.Peer ReviewedAmerican Society for Biochemistry and Molecular BiologyConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2017201720142017info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Postprintinfo:eu-repo/semantics/acceptedVersionhttp://hdl.handle.net/10261/144098reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttps://doi.org/10.1194/jlr.M049791Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/1440982026-05-22T06:33:51Z
dc.title.none.fl_str_mv Diversification of substrate specificities in teleostei Fads2: characterization of Δ4 and Δ6Δ5 desaturases of Chirostoma estor
title Diversification of substrate specificities in teleostei Fads2: characterization of Δ4 and Δ6Δ5 desaturases of Chirostoma estor
spellingShingle Diversification of substrate specificities in teleostei Fads2: characterization of Δ4 and Δ6Δ5 desaturases of Chirostoma estor
Fonseca-Madrigal, Jorge
Evolution
Fatty acyl desaturase 2
Long-chain polyunsaturated fatty acids
Teleosts
Elongase of very long-chain fatty acids
Biosynthesis
title_short Diversification of substrate specificities in teleostei Fads2: characterization of Δ4 and Δ6Δ5 desaturases of Chirostoma estor
title_full Diversification of substrate specificities in teleostei Fads2: characterization of Δ4 and Δ6Δ5 desaturases of Chirostoma estor
title_fullStr Diversification of substrate specificities in teleostei Fads2: characterization of Δ4 and Δ6Δ5 desaturases of Chirostoma estor
title_full_unstemmed Diversification of substrate specificities in teleostei Fads2: characterization of Δ4 and Δ6Δ5 desaturases of Chirostoma estor
title_sort Diversification of substrate specificities in teleostei Fads2: characterization of Δ4 and Δ6Δ5 desaturases of Chirostoma estor
dc.creator.none.fl_str_mv Fonseca-Madrigal, Jorge
Navarro, Juan Carlos
Hontoria, Francisco
Tocher, Douglas R.
Martínez-Palacios, Carlos A.
Monroig, Óscar
author Fonseca-Madrigal, Jorge
author_facet Fonseca-Madrigal, Jorge
Navarro, Juan Carlos
Hontoria, Francisco
Tocher, Douglas R.
Martínez-Palacios, Carlos A.
Monroig, Óscar
author_role author
author2 Navarro, Juan Carlos
Hontoria, Francisco
Tocher, Douglas R.
Martínez-Palacios, Carlos A.
Monroig, Óscar
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Evolution
Fatty acyl desaturase 2
Long-chain polyunsaturated fatty acids
Teleosts
Elongase of very long-chain fatty acids
Biosynthesis
topic Evolution
Fatty acyl desaturase 2
Long-chain polyunsaturated fatty acids
Teleosts
Elongase of very long-chain fatty acids
Biosynthesis
description Currently existing data show that the capability for long-chain PUFA (LC-PUFA) biosynthesis in teleost fi sh is more diverse than in other vertebrates. Such diversity has been primarily linked to the subfunctionalization that teleostei fatty acyl desaturase (Fads)2 desaturases have undergone during evolution. We previously showed that Chirostoma estor , one of the few representatives of freshwater atherinopsids, had the ability for LC-PUFA biosynthesis from C 18 PUFA precursors, in agreement with this species having unusually high contents of DHA. The particular ancestry and pattern of LC-PUFA biosynthesis activity of C. estor make this species an excellent model for study to gain further insight into LC-PUFA biosynthetic abilities among teleosts. The present study aimed to characterize cDNA sequences encoding fatty acyl elongases and desaturases, key genes involved in the LC-PUFA biosynthesis. Results show that C. estor expresses an elongase of very long-chain FA (Elovl)5 elongase and two Fads2 desaturases displaying 4 and 6/5 specifi cities, thus allowing us to conclude that these three genes cover all the enzymatic abilities required for LC-PUFA biosynthesis from C 18 PUFA. In addition, the specifi cities of the C. estor Fads2 enabled us to propose potential evolutionary patterns and mechanisms for subfunctionalization of Fads2 among fi sh lineages. -Fonseca- Madrigal, J., J. C. Navarro, F. Hontoria, D. R. Tocher, C. A. Martínez-Palacios, and Ó. Monroig. Diversifi cation of substrate specifi cities in teleostei Fads2: characterization of 4 and 6 5 desaturases of Chirostoma estor . J. Lipid Res. 2014. 55: 1408 - 1419. © 2014 by the American Society for Biochemistry and Molecular Biology, Inc.
publishDate 2014
dc.date.none.fl_str_mv 2014
2017
2017
2017
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Postprint
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/144098
url http://hdl.handle.net/10261/144098
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv https://doi.org/10.1194/jlr.M049791
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv American Society for Biochemistry and Molecular Biology
publisher.none.fl_str_mv American Society for Biochemistry and Molecular Biology
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,811543

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