An independent evolutionary origin for insect deterrent cucurbitacins in Iberis amara
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An independent evolutionary origin for insect deterrent cucurbitacins in Iberis amara. / Dong, Lemeng; Almeida Robles, Aldo Ricardo; Pollier, Jacob; Khakimov, Bekzod; Bassard, Jean-Étienne André; Miettinen, Karel; Stærk, Dan; Mehran, Rahimi; Olsen, Carl Erik; Motawie, Mohammed Saddik; Goossens, Alain; Bak, Søren.
I: Molecular Biology and Evolution, Bind 38, Nr. 11, msab213, 2021, s. 4659-4673.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - An independent evolutionary origin for insect deterrent cucurbitacins in Iberis amara
AU - Dong, Lemeng
AU - Almeida Robles, Aldo Ricardo
AU - Pollier, Jacob
AU - Khakimov, Bekzod
AU - Bassard, Jean-Étienne André
AU - Miettinen, Karel
AU - Stærk, Dan
AU - Mehran, Rahimi
AU - Olsen, Carl Erik
AU - Motawie, Mohammed Saddik
AU - Goossens, Alain
AU - Bak, Søren
PY - 2021
Y1 - 2021
N2 - Pieris rapae and Phyllotreta nemorum are Brassicaceae specialists, but do not feed on Iberis amara spp. that contain cucurbitacins. The cucurbitacins are highly oxygenated triterpenoid, occurring widespread in cucurbitaceous species and in a few other plant families. Using de novo assembled transcriptomics from I. amara, gene co-expression analysis and comparative genomics, we unraveled the evolutionary origin of the insect deterrent cucurbitacins in I. amara. Phylogenetic analysis of five oxidosqualene cyclases and heterologous expression allowed us to identify the first committed enzyme in cucurbitacin biosynthesis in I. amara, cucurbitadienol synthase (IaCPQ). In addition, two species-specific cytochrome P450s (CYP708A16 and CYP708A15) were identified that catalyze the unique C16 and C22 hydroxylation of the cucurbitadienol backbone, enzymatic steps that have not been reported before. Furthermore, the draft genome assembly of I. amara showed that the IaCPQ was localized to the same scaffold together with CYP708A15 but spanning over 100 kb, this contrasts with the highly organized cucurbitacin gene cluster in the cucurbits. These results reveal that cucurbitacin biosynthesis has evolved convergently via different biosynthetic routes in different families rather than through divergence from an ancestral pathway. This study thus provides new insight into the mechanism of recurrent evolution and diversification of a plant defensive chemical.
AB - Pieris rapae and Phyllotreta nemorum are Brassicaceae specialists, but do not feed on Iberis amara spp. that contain cucurbitacins. The cucurbitacins are highly oxygenated triterpenoid, occurring widespread in cucurbitaceous species and in a few other plant families. Using de novo assembled transcriptomics from I. amara, gene co-expression analysis and comparative genomics, we unraveled the evolutionary origin of the insect deterrent cucurbitacins in I. amara. Phylogenetic analysis of five oxidosqualene cyclases and heterologous expression allowed us to identify the first committed enzyme in cucurbitacin biosynthesis in I. amara, cucurbitadienol synthase (IaCPQ). In addition, two species-specific cytochrome P450s (CYP708A16 and CYP708A15) were identified that catalyze the unique C16 and C22 hydroxylation of the cucurbitadienol backbone, enzymatic steps that have not been reported before. Furthermore, the draft genome assembly of I. amara showed that the IaCPQ was localized to the same scaffold together with CYP708A15 but spanning over 100 kb, this contrasts with the highly organized cucurbitacin gene cluster in the cucurbits. These results reveal that cucurbitacin biosynthesis has evolved convergently via different biosynthetic routes in different families rather than through divergence from an ancestral pathway. This study thus provides new insight into the mechanism of recurrent evolution and diversification of a plant defensive chemical.
U2 - 10.1093/molbev/msab213
DO - 10.1093/molbev/msab213
M3 - Journal article
C2 - 34264303
VL - 38
SP - 4659
EP - 4673
JO - Molecular Biology and Evolution
JF - Molecular Biology and Evolution
SN - 0737-4038
IS - 11
M1 - msab213
ER -
ID: 274069705