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Journal Article

Contribution of CoA ligases to benzenoid biosynthesis in Petunia flowers


D'Auria,  John
Department of Biochemistry, Prof. J. Gershenzon, MPI for Chemical Ecology, Max Planck Society;

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Klempien, A., Kaminaga, Y., Qualley, A., Nagegowda, D. A., Widhalm, J. R., Orlova, I., et al. (2012). Contribution of CoA ligases to benzenoid biosynthesis in Petunia flowers. The Plant Cell, 24(5), 2015-2030. doi:10.1105/tpc.112.097519.

Cite as: https://hdl.handle.net/11858/00-001M-0000-000F-A081-4
Biosynthesis of benzoic acid from Phe requires shortening of the side chain by two carbons, which can occur via the β-oxidative or nonoxidative pathways. The first step in the β-oxidative pathway is cinnamoyl-CoA formation, likely catalyzed by a member of the 4-coumarate:CoA ligase (4CL) family that converts a range of trans-cinnamic acid derivatives into the corresponding CoA thioesters. Using a functional genomics approach, we identified two potential CoA-ligases from petunia (Petunia hybrida) petal-specific cDNA libraries. The cognate proteins share only 25% amino acid identity and are highly expressed in petunia corollas. Biochemical characterization of the recombinant proteins revealed that one of these proteins (Ph-4CL1) has broad substrate specificity and represents a bona fide 4CL, whereas the other is a cinnamate:CoA ligase (Ph-CNL). RNA interference suppression of Ph-4CL1 did not affect the petunia benzenoid scent profile, whereas downregulation of Ph-CNL resulted in a decrease in emission of benzylbenzoate, phenylethylbenzoate, and methylbenzoate. Green fluorescent protein localization studies revealed that the Ph-4CL1 protein is localized in the cytosol, whereas Ph-CNL is in peroxisomes. Our results indicate that subcellular compartmentalization of enzymes affects their involvement in the benzenoid network and provide evidence that cinnamoyl-CoA formation by Ph-CNL in the peroxisomes is the committed step in the β-oxidative pathway.