Enzymatic study on AtCCD4 and AtCCD7 and their potential to form acyclic regulatory metabolites

Handle URI:
http://hdl.handle.net/10754/621841
Title:
Enzymatic study on AtCCD4 and AtCCD7 and their potential to form acyclic regulatory metabolites
Authors:
Bruno, Mark; Koschmieder, Julian; Wuest, Florian; Schaub, Patrick; Fehling-Kaschek, Mirjam; Timmer, Jens; Beyer, Peter; Al-Babili, Salim ( 0000-0003-4823-2882 )
Abstract:
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.
KAUST Department:
Biological and Environmental Sciences and Engineering (BESE) Division; Center for Desert Agriculture
Citation:
Bruno M, Koschmieder J, Wuest F, Schaub P, Fehling-Kaschek M, et al. (2016) Enzymatic study on AtCCD4 and AtCCD7 and their potential to form acyclic regulatory metabolites. Journal of Experimental Botany 67: 5993–6005. Available: http://dx.doi.org/10.1093/jxb/erw356.
Publisher:
Oxford University Press (OUP)
Journal:
Journal of Experimental Botany
Issue Date:
29-Sep-2016
DOI:
10.1093/jxb/erw356
Type:
Article
ISSN:
0022-0957; 1460-2431
Sponsors:
This work was supported by the European Union (METAPRO; FP7 KBBE-2009-3-1-01) and the King Abdullah University of Science and Technology (KAUST).
Additional Links:
http://dx.doi.org/10.1093/jxb/erw356
Appears in Collections:
Articles; Center for Desert Agriculture; Biological and Environmental Sciences and Engineering (BESE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorBruno, Marken
dc.contributor.authorKoschmieder, Julianen
dc.contributor.authorWuest, Florianen
dc.contributor.authorSchaub, Patricken
dc.contributor.authorFehling-Kaschek, Mirjamen
dc.contributor.authorTimmer, Jensen
dc.contributor.authorBeyer, Peteren
dc.contributor.authorAl-Babili, Salimen
dc.date.accessioned2016-11-21T06:21:07Z-
dc.date.available2016-11-21T06:21:07Z-
dc.date.issued2016-09-29en
dc.identifier.citationBruno M, Koschmieder J, Wuest F, Schaub P, Fehling-Kaschek M, et al. (2016) Enzymatic study on AtCCD4 and AtCCD7 and their potential to form acyclic regulatory metabolites. Journal of Experimental Botany 67: 5993–6005. Available: http://dx.doi.org/10.1093/jxb/erw356.en
dc.identifier.issn0022-0957en
dc.identifier.issn1460-2431en
dc.identifier.doi10.1093/jxb/erw356en
dc.identifier.urihttp://hdl.handle.net/10754/621841-
dc.description.abstractThe 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.en
dc.description.sponsorshipThis work was supported by the European Union (METAPRO; FP7 KBBE-2009-3-1-01) and the King Abdullah University of Science and Technology (KAUST).en
dc.publisherOxford University Press (OUP)en
dc.relation.urlhttp://dx.doi.org/10.1093/jxb/erw356en
dc.rightsThis 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.en
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/en
dc.subjectApocarotenoidsen
dc.subjectcarotenoidsen
dc.subjectcarotenoid cleavage dioxygenaseen
dc.subjectCCD4en
dc.subjectCCD7en
dc.subjectretrograde signalingen
dc.titleEnzymatic study on AtCCD4 and AtCCD7 and their potential to form acyclic regulatory metabolitesen
dc.typeArticleen
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Divisionen
dc.contributor.departmentCenter for Desert Agricultureen
dc.identifier.journalJournal of Experimental Botanyen
dc.eprint.versionPublisher's Version/PDFen
dc.contributor.institutionAlbert-Ludwigs University of Freiburg, Faculty of Biology, Schaenzlestr. 1, D-79104 Freiburg, Germanyen
dc.contributor.institutionAlbert-Ludwigs University of Freiburg, Department of Physics, Hermann-Herder-Str. 3a, D-79104 Freiburg, Germanyen
dc.contributor.institutionAlbert-Ludwigs University of Freiburg, BIOSS Center for Biological Signalling Studies, Schaenzlestr. 18, D-79104 Freiburg, Germanyen
kaust.authorAl-Babili, Salimen
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