Phylogenetic analysis of the metazoan carotenoid oxygenase superfamily: a new ancestral gene assemblage of BCO-like (BCOL) proteins
Abstract Here we describe a new family of carotenoid cleavage oxygenases (CCOs) in metazoans, the BCO2-like (BCOL) clade, which contains lancelet, nematode, and molluscan carotenoid oxygenase sequences. Phylogenetic analysis of CCOs in all kingdoms of life confirmed that the BCOL enzymes are an inde...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2017-10-01
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| Series: | Scientific Reports |
| Online Access: | https://doi.org/10.1038/s41598-017-13521-x |
| _version_ | 1818840732714139648 |
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| author | Eugenia Poliakov Joseph Soucy Susan Gentleman Igor B. Rogozin T. Michael Redmond |
| author_facet | Eugenia Poliakov Joseph Soucy Susan Gentleman Igor B. Rogozin T. Michael Redmond |
| author_sort | Eugenia Poliakov |
| collection | DOAJ |
| description | Abstract Here we describe a new family of carotenoid cleavage oxygenases (CCOs) in metazoans, the BCO2-like (BCOL) clade, which contains lancelet, nematode, and molluscan carotenoid oxygenase sequences. Phylogenetic analysis of CCOs in all kingdoms of life confirmed that the BCOL enzymes are an independent clade of ancient origin. One of the predicted lancelet BCOL proteins, cloned and analyzed for carotenoid cleavage activity in a bacterial carotenoid expression system, had activity similar to lancelet BCO2 proteins, although with a preference for cis isomers. Our docking predictions correlated well with the cis-favored activity. The extensive expansions of the new animal BCOL family in some species (e.g., lancelet) suggests that the carotenoid cleavage oxygenase superfamily has evolved in the “extremely high turnover” fashion: numerous losses and duplications of this family are likely to reflect complex regulation processes during development, and interactions with the environment. These findings also serve to provide a rationale for the evolution of the BCO-related outlier RPE65 retinol isomerase, an enzyme that does not utilize carotenoids as substrate or perform double-bond cleavage. |
| first_indexed | 2024-12-19T04:14:52Z |
| format | Article |
| id | doaj.art-f411c555a86b4c2490a23365c5dbfb0d |
| institution | Directory Open Access Journal |
| issn | 2045-2322 |
| language | English |
| last_indexed | 2024-12-19T04:14:52Z |
| publishDate | 2017-10-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Scientific Reports |
| spelling | doaj.art-f411c555a86b4c2490a23365c5dbfb0d2022-12-21T20:36:20ZengNature PortfolioScientific Reports2045-23222017-10-017111210.1038/s41598-017-13521-xPhylogenetic analysis of the metazoan carotenoid oxygenase superfamily: a new ancestral gene assemblage of BCO-like (BCOL) proteinsEugenia Poliakov0Joseph Soucy1Susan Gentleman2Igor B. Rogozin3T. Michael Redmond4Laboratory of Retinal Cell & Molecular Biology, National Eye Institute, National Institutes of HealthLaboratory of Retinal Cell & Molecular Biology, National Eye Institute, National Institutes of HealthLaboratory of Retinal Cell & Molecular Biology, National Eye Institute, National Institutes of HealthNational Center for Biotechnology Information, National Library of Medicine, National Institutes of HealthLaboratory of Retinal Cell & Molecular Biology, National Eye Institute, National Institutes of HealthAbstract Here we describe a new family of carotenoid cleavage oxygenases (CCOs) in metazoans, the BCO2-like (BCOL) clade, which contains lancelet, nematode, and molluscan carotenoid oxygenase sequences. Phylogenetic analysis of CCOs in all kingdoms of life confirmed that the BCOL enzymes are an independent clade of ancient origin. One of the predicted lancelet BCOL proteins, cloned and analyzed for carotenoid cleavage activity in a bacterial carotenoid expression system, had activity similar to lancelet BCO2 proteins, although with a preference for cis isomers. Our docking predictions correlated well with the cis-favored activity. The extensive expansions of the new animal BCOL family in some species (e.g., lancelet) suggests that the carotenoid cleavage oxygenase superfamily has evolved in the “extremely high turnover” fashion: numerous losses and duplications of this family are likely to reflect complex regulation processes during development, and interactions with the environment. These findings also serve to provide a rationale for the evolution of the BCO-related outlier RPE65 retinol isomerase, an enzyme that does not utilize carotenoids as substrate or perform double-bond cleavage.https://doi.org/10.1038/s41598-017-13521-x |
| spellingShingle | Eugenia Poliakov Joseph Soucy Susan Gentleman Igor B. Rogozin T. Michael Redmond Phylogenetic analysis of the metazoan carotenoid oxygenase superfamily: a new ancestral gene assemblage of BCO-like (BCOL) proteins Scientific Reports |
| title | Phylogenetic analysis of the metazoan carotenoid oxygenase superfamily: a new ancestral gene assemblage of BCO-like (BCOL) proteins |
| title_full | Phylogenetic analysis of the metazoan carotenoid oxygenase superfamily: a new ancestral gene assemblage of BCO-like (BCOL) proteins |
| title_fullStr | Phylogenetic analysis of the metazoan carotenoid oxygenase superfamily: a new ancestral gene assemblage of BCO-like (BCOL) proteins |
| title_full_unstemmed | Phylogenetic analysis of the metazoan carotenoid oxygenase superfamily: a new ancestral gene assemblage of BCO-like (BCOL) proteins |
| title_short | Phylogenetic analysis of the metazoan carotenoid oxygenase superfamily: a new ancestral gene assemblage of BCO-like (BCOL) proteins |
| title_sort | phylogenetic analysis of the metazoan carotenoid oxygenase superfamily a new ancestral gene assemblage of bco like bcol proteins |
| url | https://doi.org/10.1038/s41598-017-13521-x |
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