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Abstract Detail


Secondary Metabolism

Dudareva, Natalia [1], Qualley, Anthony [2].

Protein-Protein interactions are involved in eugenol and isoeugenol biosynthesis in Petunia.

Eugenol and isoeugenol are compounds valued for their fragrance, flavor, and food-preserving properties. It has previously been demonstrated that both volatiles are produced from coniferyl alcohol through a two-step reaction involving the acetylation of the alcohol and subsequent reduction to eugenol/isoeugnol. The two proteins responsible for these reactions (PhCFAT and PhEGS/IGS) have been isolated and characterized in vitro, but evidence suggests that protein-protein interactions between these enzymes are essential for product formation due to the inherent instability of the acetylated intermediate as a result of facile quinone methide formation. The goal of this study is to confirm the possible formation, stability, affinity and catalytic properties of this putative CFAT-EGS/IGS complex using complementary in vivo and in vitro techniques. We hypothesize that CFAT and EGS/IGS function through protein-protein interactions to enable reduction of the unstable acetylated intermediate. Preliminary in vitro co-expression of the affinity tagged CFAT protein with untagged IGS indicates that these proteins interact and co-purify on Ni2+-NTA resins. Elucidation of this final step in the biosynthesis of eugenol and isoeugenol will allow us to attempt genetic modification of plants for the production of these compounds.


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1 - Purdue University, Department of Horticulture and Landscape Architecture, 625, Agricultural Mall drive, Purdue University, West Lafayette, IN, 47907, USA
2 - Purdue University, Department of Horticulture and Landscape Architecture, 625 Agriculture Mall Dr., West Lafayette, IN, 47907-2010, USA

Keywords:
secondary metabolism
Petunia
eugenol
isoeugenol
protein-protein interaction.

Presentation Type: Plant Biology Abstract
Session: P
Location: Exhibit Hall (Northeast, Southwest & Southeast)/Hilton
Date: Sunday, July 8th, 2007
Time: 8:00 AM
Number: P20013
Abstract ID:246


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