A mechanism for red coloration in vertebrates

Bibliographic Details
Main Author: Toomey, Matthew B.
Publication Date: 2022
Other Authors: 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.
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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spelling 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
instname_str FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologia
instacron_str RCAAP
institution RCAAP
reponame_str Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
collection Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
repository.name.fl_str_mv 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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