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Enzymatic study on AtCCD4 and AtCCD7 and their potential to form acyclic regulatory metabolites
The Arabidopsis carotenoid cleavage dioxygenase 4 (AtCCD4) is a negative regulator of the carotenoid content of seeds and has recently been suggested as a candidate for the generation of retrograde signals that are thought to derive from the cleavage of poly-cis-configured carotene desaturation inte...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5100015/ https://www.ncbi.nlm.nih.gov/pubmed/27811075 http://dx.doi.org/10.1093/jxb/erw356 |
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author | Bruno, Mark Koschmieder, Julian Wuest, Florian Schaub, Patrick Fehling-Kaschek, Mirjam Timmer, Jens Beyer, Peter Al-Babili, Salim |
author_facet | Bruno, Mark Koschmieder, Julian Wuest, Florian Schaub, Patrick Fehling-Kaschek, Mirjam Timmer, Jens Beyer, Peter Al-Babili, Salim |
author_sort | Bruno, Mark |
collection | PubMed |
description | The Arabidopsis carotenoid cleavage dioxygenase 4 (AtCCD4) is a negative regulator of the carotenoid content of seeds and has recently been suggested as a candidate for the generation of retrograde signals that are thought to derive from the cleavage of poly-cis-configured carotene desaturation intermediates. In this work, we investigated the activity of AtCCD4 in vitro and used dynamic modeling to determine its substrate preference. Our results document strict regional specificity for cleavage at the C9–C10 double bond in carotenoids and apocarotenoids, with preference for carotenoid substrates and an obstructing effect on hydroxyl functions, and demonstrate the specificity for all-trans-configured carotenes and xanthophylls. AtCCD4 cleaved substrates with at least one ionone ring and did not convert acyclic carotene desaturation intermediates, independent of their isomeric states. These results do not support a direct involvement of AtCCD4 in generating the supposed regulatory metabolites. In contrast, the strigolactone biosynthetic enzyme AtCCD7 converted 9-cis-configured acyclic carotenes, such as 9-cis-ζ-carotene, 9'-cis-neurosporene, and 9-cis-lycopene, yielding 9-cis-configured products and indicating that AtCCD7, rather than AtCCD4, is the candidate for forming acyclic retrograde signals. |
format | Online Article Text |
id | pubmed-5100015 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-51000152016-11-10 Enzymatic study on AtCCD4 and AtCCD7 and their potential to form acyclic regulatory metabolites Bruno, Mark Koschmieder, Julian Wuest, Florian Schaub, Patrick Fehling-Kaschek, Mirjam Timmer, Jens Beyer, Peter Al-Babili, Salim J Exp Bot Research Paper The Arabidopsis carotenoid cleavage dioxygenase 4 (AtCCD4) is a negative regulator of the carotenoid content of seeds and has recently been suggested as a candidate for the generation of retrograde signals that are thought to derive from the cleavage of poly-cis-configured carotene desaturation intermediates. In this work, we investigated the activity of AtCCD4 in vitro and used dynamic modeling to determine its substrate preference. Our results document strict regional specificity for cleavage at the C9–C10 double bond in carotenoids and apocarotenoids, with preference for carotenoid substrates and an obstructing effect on hydroxyl functions, and demonstrate the specificity for all-trans-configured carotenes and xanthophylls. AtCCD4 cleaved substrates with at least one ionone ring and did not convert acyclic carotene desaturation intermediates, independent of their isomeric states. These results do not support a direct involvement of AtCCD4 in generating the supposed regulatory metabolites. In contrast, the strigolactone biosynthetic enzyme AtCCD7 converted 9-cis-configured acyclic carotenes, such as 9-cis-ζ-carotene, 9'-cis-neurosporene, and 9-cis-lycopene, yielding 9-cis-configured products and indicating that AtCCD7, rather than AtCCD4, is the candidate for forming acyclic retrograde signals. Oxford University Press 2016-11 2016-10-06 /pmc/articles/PMC5100015/ /pubmed/27811075 http://dx.doi.org/10.1093/jxb/erw356 Text en © The Author 2016. Published by Oxford University Press on behalf of the Society for Experimental Biology. http://creativecommons.org/licenses/by/3.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Paper Bruno, Mark Koschmieder, Julian Wuest, Florian Schaub, Patrick Fehling-Kaschek, Mirjam Timmer, Jens Beyer, Peter Al-Babili, Salim Enzymatic study on AtCCD4 and AtCCD7 and their potential to form acyclic regulatory metabolites |
title | Enzymatic study on AtCCD4 and AtCCD7 and their potential to form acyclic regulatory metabolites |
title_full | Enzymatic study on AtCCD4 and AtCCD7 and their potential to form acyclic regulatory metabolites |
title_fullStr | Enzymatic study on AtCCD4 and AtCCD7 and their potential to form acyclic regulatory metabolites |
title_full_unstemmed | Enzymatic study on AtCCD4 and AtCCD7 and their potential to form acyclic regulatory metabolites |
title_short | Enzymatic study on AtCCD4 and AtCCD7 and their potential to form acyclic regulatory metabolites |
title_sort | enzymatic study on atccd4 and atccd7 and their potential to form acyclic regulatory metabolites |
topic | Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5100015/ https://www.ncbi.nlm.nih.gov/pubmed/27811075 http://dx.doi.org/10.1093/jxb/erw356 |
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