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Acquired immunity of transgenic torenia plants overexpressing agmatine coumaroyltransferase to pathogens and herbivore pests.


ABSTRACT: We investigated the ability of transgenic torenia (Scrophulariaceae) plants to resist fungi and arthropod herbivores. Torenia hybrida cv. Summerwave Blue was manipulated to produce Arabidopsis agmatine coumaroyltransferase (AtACT). This catalyses the last step in the biosynthesis of hydroxycinnamic acid amides (HCAAs) which function in defence. Transgenic plants accumulated substantial HCAAs, predominantly p-coumaroylagmatine, and the HCAAs were isomerized from the trans-form to the cis-form in planta. The transgenic line, accumulated the highest amount of endogenous HCAAs (CouAgm at 32.2 µM and total HCAAs at 47.5 µM) and this line was resistant to the necrotrophic fungus, Botrytis cinerea. There was no resistance, however, in their wild-type progenitors or in other transgenic lines accumulating low HCAA amounts. In contrast, the transformants were not significantly resistant to three representative herbivores, Frankliniella occidentalis, Aphis gossypii, and Tetranychus ludeni.

SUBMITTER: Muroi A 

PROVIDER: S-EPMC3449287 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature

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Acquired immunity of transgenic torenia plants overexpressing agmatine coumaroyltransferase to pathogens and herbivore pests.

Muroi Atsushi A   Matsui Kenji K   Shimoda Takeshi T   Kihara Hirotomo H   Ozawa Rika R   Ishihara Atsushi A   Nishihara Masahiro M   Arimura Gen-ichiro G  

Scientific reports 20120924


We investigated the ability of transgenic torenia (Scrophulariaceae) plants to resist fungi and arthropod herbivores. Torenia hybrida cv. Summerwave Blue was manipulated to produce Arabidopsis agmatine coumaroyltransferase (AtACT). This catalyses the last step in the biosynthesis of hydroxycinnamic acid amides (HCAAs) which function in defence. Transgenic plants accumulated substantial HCAAs, predominantly p-coumaroylagmatine, and the HCAAs were isomerized from the trans-form to the cis-form in  ...[more]

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