Journal
PLANTA
Volume 230, Issue 3, Pages 517-527Publisher
SPRINGER
DOI: 10.1007/s00425-009-0960-0
Keywords
Arabidopsis thaliana; Alternaria brassicicola; HCAA; p-Coumaroylagmatine; Agmatine coumaroyltransferase; BAHD acyltransferase family
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Funding
- Japan Society for the Promotion of Science [18380066, 21580126]
- Grants-in-Aid for Scientific Research [21580126, 19101009, 18380066] Funding Source: KAKEN
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Hydroxycinnamic acid amides (HCAAs) are secondary metabolites involved in the defense of plants against pathogens. Here, we report the first identification of HCAAs, p-coumaroylagmatine, feruloylagmatine, p-coumaroylputrescine and feruloylputrescine, in Arabidopsis thaliana rosette leaves infected with Alternaria brassicicola and the assignment of At5g61160 as the agmatine coumaroyltransferase (AtACT) that catalyzes the last reaction in the biosynthesis of the HCAAs. Feeding experiments with putative labeled precursors revealed that the four HCAAs were synthesized from hydroxycinnamic acids and agmatine or putrescine. AtACT gene function was identified from an analysis of a mutant that did not accumulate HCAAs. In wild-type Arabidopsis, AtACT transcripts markedly increased in response to A. brassicicola infection. Enzymatic activity that catalyzes the synthesis of the HCAAs was confirmed in vitro by using a recombinant AtACT expressed in Escherichia coli. The Atact mutant was susceptible to infection by A. brassicicola, indicating that HCAAs are responsible for defense against pathogens in A. thaliana.
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