TY - JOUR

T1 - Distinct triterpene synthases in the laticifers of Euphorbia lathyris

AU - Forestier, Edith

AU - Romero-Segura, Carmen

AU - Pateraki, Irini

AU - Centeno, Emilio

AU - Compagnon, Vincent

AU - Preiss, Myriam

AU - Berna, Anne

AU - Boronat, Albert

AU - Bach, Thomas J.

AU - Darnet, Sylvain

AU - Schaller, Hubert

N1 - Funding Information: The authors are grateful to Profs. Yukuta Ebizuka and Tetsuo Kushiro for a gift of the GIL77 (erg7) yeast strain, to Dr. Pascaline Ullmann for valuable advice on yeast transformation, to Dr. Raphaël Lugan and Dr. Dimitri Heintz for GC-MS implementation, and to Dr. Bruno Vincent for NMR analysis. This work was funded by a Plant Knowledge Based Bio Economy program ‘EULAFUEL’ (Plant KBBE 2009–2014) to Prof. Thomas J. Bach and Dr. Hubert Schaller (ANR09-KBBE-003-002), and to Prof. Albert Boronat (PLE2009-0003 from Ministerio de Ciencia e Innovación, Spain). The cooperation between Universidade Federal do Pará, Belém, Brazil, and the Institut de Biologie Moléculaire des Plantes is framed by a French-Brazilian International Associated Laboratory LIA N°1170 (Palmheat, Drs Sylvain Darnet and Hubert Schaller). Publisher Copyright: © 2019, The Author(s).

PY - 2019

Y1 - 2019

N2 - Euphorbia lathyris was proposed about fifty years ago as a potential agroenergetic crop. The tremendous amounts of triterpenes present in its latex has driven investigations for transforming this particular biological fluid into an industrial hydrocarbon source. The huge accumulation of terpenes in the latex of many plant species represent a challenging question regarding cellular homeostasis. In fact, the enzymes, the mechanisms and the controllers that tune the amount of products accumulated in specialized compartments (to fulfill ecological roles) or deposited at important sites (as essential factors) are not known. Here, we have isolated oxidosqualene cyclases highly expressed in the latex of Euphorbia lathyris. This triterpene biosynthetic machinery is made of distinct paralogous enzymes responsible for the massive accumulation of steroidal and non-steroidal tetracyclic triterpenes. More than eighty years after the isolation of butyrospermol from shea butter (Heilbronn IM, Moffet GL, and Spring FS J. Chem. Soc. 1934, 1583), a butyrospermol synthase is characterized in this work using yeast and in folia heterologous expression assays.

AB - Euphorbia lathyris was proposed about fifty years ago as a potential agroenergetic crop. The tremendous amounts of triterpenes present in its latex has driven investigations for transforming this particular biological fluid into an industrial hydrocarbon source. The huge accumulation of terpenes in the latex of many plant species represent a challenging question regarding cellular homeostasis. In fact, the enzymes, the mechanisms and the controllers that tune the amount of products accumulated in specialized compartments (to fulfill ecological roles) or deposited at important sites (as essential factors) are not known. Here, we have isolated oxidosqualene cyclases highly expressed in the latex of Euphorbia lathyris. This triterpene biosynthetic machinery is made of distinct paralogous enzymes responsible for the massive accumulation of steroidal and non-steroidal tetracyclic triterpenes. More than eighty years after the isolation of butyrospermol from shea butter (Heilbronn IM, Moffet GL, and Spring FS J. Chem. Soc. 1934, 1583), a butyrospermol synthase is characterized in this work using yeast and in folia heterologous expression assays.

U2 - 10.1038/s41598-019-40905-y

DO - 10.1038/s41598-019-40905-y

M3 - Journal article

C2 - 30886213

AN - SCOPUS:85063035603

VL - 9

JO - Scientific Reports

JF - Scientific Reports

SN - 2045-2322

IS - 1

M1 - 4840

ER -