An algal enzyme required for biosynthesis of the most abundant marine carotenoids
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An algal enzyme required for biosynthesis of the most abundant marine carotenoids. / Dautermann, O.; Lyska, D.; Andersen-Ranberg, J.; Becker, M.; Fröhlich-Nowoisky, J.; Gartmann, H.; Krämer, L. C.; Mayr, K.; Pieper, D.; Rij, L. M.; Wipf, H. M.L.; Niyogi, K. K.; Lohr, M.
In: Science Advances, Vol. 6, No. 10, eaaw9183, 2020.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - An algal enzyme required for biosynthesis of the most abundant marine carotenoids
AU - Dautermann, O.
AU - Lyska, D.
AU - Andersen-Ranberg, J.
AU - Becker, M.
AU - Fröhlich-Nowoisky, J.
AU - Gartmann, H.
AU - Krämer, L. C.
AU - Mayr, K.
AU - Pieper, D.
AU - Rij, L. M.
AU - Wipf, H. M.L.
AU - Niyogi, K. K.
AU - Lohr, M.
N1 - Publisher Copyright: © 2020 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution License 4.0 (CC BY).
PY - 2020
Y1 - 2020
N2 - Fucoxanthin and its derivatives are the main light-harvesting pigments in the photosynthetic apparatus of many chromalveolate algae and represent the most abundant carotenoids in the world's oceans, thus being major facilitators of marine primary production. A central step in fucoxanthin biosynthesis that has been elusive so far is the conversion of violaxanthin to neoxanthin. Here, we show that in chromalveolates, this reaction is catalyzed by violaxanthin de-epoxidase-like (VDL) proteins and that VDL is also involved in the formation of other light-harvesting carotenoids such as peridinin or vaucheriaxanthin. VDL is closely related to the photoprotective enzyme violaxanthin de-epoxidase that operates in plants and most algae, revealing that in major phyla of marine algae, an ancient gene duplication triggered the evolution of carotenoid functions beyond photoprotection toward light harvesting.
AB - Fucoxanthin and its derivatives are the main light-harvesting pigments in the photosynthetic apparatus of many chromalveolate algae and represent the most abundant carotenoids in the world's oceans, thus being major facilitators of marine primary production. A central step in fucoxanthin biosynthesis that has been elusive so far is the conversion of violaxanthin to neoxanthin. Here, we show that in chromalveolates, this reaction is catalyzed by violaxanthin de-epoxidase-like (VDL) proteins and that VDL is also involved in the formation of other light-harvesting carotenoids such as peridinin or vaucheriaxanthin. VDL is closely related to the photoprotective enzyme violaxanthin de-epoxidase that operates in plants and most algae, revealing that in major phyla of marine algae, an ancient gene duplication triggered the evolution of carotenoid functions beyond photoprotection toward light harvesting.
U2 - 10.1126/sciadv.aaw9183
DO - 10.1126/sciadv.aaw9183
M3 - Journal article
C2 - 32181334
AN - SCOPUS:85081962098
VL - 6
JO - Science advances
JF - Science advances
SN - 2375-2548
IS - 10
M1 - eaaw9183
ER -
ID: 273295832