A mechanism for red coloration in vertebrates
Main Author: | |
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Publication Date: | 2022 |
Other Authors: | , , , , , , , , , , , , , , , , , , , , , |
Format: | Article |
Language: | eng |
Source: | Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) |
Download full: | https://hdl.handle.net/10316/101618 https://doi.org/10.1016/j.cub.2022.08.013 |
Summary: | Red coloration is a salient feature of the natural world. Many vertebrates produce red color by converting dietary yellow carotenoids into red ketocarotenoids via an unknown mechanism. Here, we show that two enzymes, cytochrome P450 2J19 (CYP2J19) and 3-hydroxybutyrate dehydrogenase 1-like (BDH1L), are sufficient to catalyze this conversion. In birds, both enzymes are expressed at the sites of ketocarotenoid biosynthesis (feather follicles and red cone photoreceptors), and genetic evidence implicates these enzymes in yellow/red color variation in feathers. In fish, the homologs of CYP2J19 and BDH1L are required for ketocarotenoid production, and we show that these enzymes are sufficient to produce ketocarotenoids in cell culture and when ectopically expressed in fish skin. Finally, we demonstrate that the red-cone-enriched tetratricopeptide repeat protein 39B (TTC39B) enhances ketocarotenoid production when co-expressed with CYP2J19 and BDH1L. The discovery of this mechanism of ketocarotenoid biosynthesis has major implications for understanding the evolution of color diversity in vertebrates. |
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A mechanism for red coloration in vertebratesRed coloration is a salient feature of the natural world. Many vertebrates produce red color by converting dietary yellow carotenoids into red ketocarotenoids via an unknown mechanism. Here, we show that two enzymes, cytochrome P450 2J19 (CYP2J19) and 3-hydroxybutyrate dehydrogenase 1-like (BDH1L), are sufficient to catalyze this conversion. In birds, both enzymes are expressed at the sites of ketocarotenoid biosynthesis (feather follicles and red cone photoreceptors), and genetic evidence implicates these enzymes in yellow/red color variation in feathers. In fish, the homologs of CYP2J19 and BDH1L are required for ketocarotenoid production, and we show that these enzymes are sufficient to produce ketocarotenoids in cell culture and when ectopically expressed in fish skin. Finally, we demonstrate that the red-cone-enriched tetratricopeptide repeat protein 39B (TTC39B) enhances ketocarotenoid production when co-expressed with CYP2J19 and BDH1L. The discovery of this mechanism of ketocarotenoid biosynthesis has major implications for understanding the evolution of color diversity in vertebrates.Elsevier; Cell Press2022-08-25info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlehttps://hdl.handle.net/10316/101618https://hdl.handle.net/10316/101618https://doi.org/10.1016/j.cub.2022.08.013eng09609822https://www.sciencedirect.com/science/article/pii/S0960982222012908Toomey, Matthew B.Marques, Cristiana I.Araújo, Pedro M.Huang, DelaiZhong, SiqiongLiu, YuSchreiner, Gretchen D.Myers, Connie A.Pereira, PauloAfonso, SandraAndrade, PedroGazda, Małgorzata A.Lopes, Ricardo J.Viegas, IvanKoch, Rebecca E.Haynes, Maureen E.Smith, Dustin J.Ogawa, YoheyMurphy, DanielKopec, Rachel E.Parichy, David M.Carneiro, Miguel .Corbo, Joseph C.info:eu-repo/semantics/openAccessreponame:Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)instname:FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiainstacron:RCAAP2024-01-02T11:22:49Zoai:estudogeral.uc.pt:10316/101618Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireinfo@rcaap.ptopendoar:https://opendoar.ac.uk/repository/71602025-05-29T05:51:01.026298Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) - FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiafalse |
dc.title.none.fl_str_mv |
A mechanism for red coloration in vertebrates |
title |
A mechanism for red coloration in vertebrates |
spellingShingle |
A mechanism for red coloration in vertebrates Toomey, Matthew B. |
title_short |
A mechanism for red coloration in vertebrates |
title_full |
A mechanism for red coloration in vertebrates |
title_fullStr |
A mechanism for red coloration in vertebrates |
title_full_unstemmed |
A mechanism for red coloration in vertebrates |
title_sort |
A mechanism for red coloration in vertebrates |
author |
Toomey, Matthew B. |
author_facet |
Toomey, Matthew B. Marques, Cristiana I. Araújo, Pedro M. Huang, Delai Zhong, Siqiong Liu, Yu Schreiner, Gretchen D. Myers, Connie A. Pereira, Paulo Afonso, Sandra Andrade, Pedro Gazda, Małgorzata A. Lopes, Ricardo J. Viegas, Ivan Koch, Rebecca E. Haynes, Maureen E. Smith, Dustin J. Ogawa, Yohey Murphy, Daniel Kopec, Rachel E. Parichy, David M. Carneiro, Miguel . Corbo, Joseph C. |
author_role |
author |
author2 |
Marques, Cristiana I. Araújo, Pedro M. Huang, Delai Zhong, Siqiong Liu, Yu Schreiner, Gretchen D. Myers, Connie A. Pereira, Paulo Afonso, Sandra Andrade, Pedro Gazda, Małgorzata A. Lopes, Ricardo J. Viegas, Ivan Koch, Rebecca E. Haynes, Maureen E. Smith, Dustin J. Ogawa, Yohey Murphy, Daniel Kopec, Rachel E. Parichy, David M. Carneiro, Miguel . Corbo, Joseph C. |
author2_role |
author author author author author author author author author author author author author author author author author author author author author author |
dc.contributor.author.fl_str_mv |
Toomey, Matthew B. Marques, Cristiana I. Araújo, Pedro M. Huang, Delai Zhong, Siqiong Liu, Yu Schreiner, Gretchen D. Myers, Connie A. Pereira, Paulo Afonso, Sandra Andrade, Pedro Gazda, Małgorzata A. Lopes, Ricardo J. Viegas, Ivan Koch, Rebecca E. Haynes, Maureen E. Smith, Dustin J. Ogawa, Yohey Murphy, Daniel Kopec, Rachel E. Parichy, David M. Carneiro, Miguel . Corbo, Joseph C. |
description |
Red coloration is a salient feature of the natural world. Many vertebrates produce red color by converting dietary yellow carotenoids into red ketocarotenoids via an unknown mechanism. Here, we show that two enzymes, cytochrome P450 2J19 (CYP2J19) and 3-hydroxybutyrate dehydrogenase 1-like (BDH1L), are sufficient to catalyze this conversion. In birds, both enzymes are expressed at the sites of ketocarotenoid biosynthesis (feather follicles and red cone photoreceptors), and genetic evidence implicates these enzymes in yellow/red color variation in feathers. In fish, the homologs of CYP2J19 and BDH1L are required for ketocarotenoid production, and we show that these enzymes are sufficient to produce ketocarotenoids in cell culture and when ectopically expressed in fish skin. Finally, we demonstrate that the red-cone-enriched tetratricopeptide repeat protein 39B (TTC39B) enhances ketocarotenoid production when co-expressed with CYP2J19 and BDH1L. The discovery of this mechanism of ketocarotenoid biosynthesis has major implications for understanding the evolution of color diversity in vertebrates. |
publishDate |
2022 |
dc.date.none.fl_str_mv |
2022-08-25 |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
https://hdl.handle.net/10316/101618 https://hdl.handle.net/10316/101618 https://doi.org/10.1016/j.cub.2022.08.013 |
url |
https://hdl.handle.net/10316/101618 https://doi.org/10.1016/j.cub.2022.08.013 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
09609822 https://www.sciencedirect.com/science/article/pii/S0960982222012908 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.publisher.none.fl_str_mv |
Elsevier; Cell Press |
publisher.none.fl_str_mv |
Elsevier; Cell Press |
dc.source.none.fl_str_mv |
reponame:Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) instname:FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologia instacron:RCAAP |
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FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologia |
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RCAAP |
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RCAAP |
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Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) |
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Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) |
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Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) - FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologia |
repository.mail.fl_str_mv |
info@rcaap.pt |
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