Proteomics

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Benzyl alcohol biosynthesis and its subcellular compartmentalization: from scent formation to salicylic acid production


ABSTRACT: Benzyl alcohol, a simple aromatic alcohol found in more than half of seed plants, plays important roles in plant-environmental interactions and serves as a precursor of benzyl benzoate, an intermediate in the phenylalanine-dependent salicylic acid biosynthesis. Despite its importance, the enzyme responsible for its formation in plants has remained unknown. Here, using a combination of classical biochemical, proteomic and genetic approaches, we demonstrated that two NADPH-dependent benzaldehyde reductases, differing by only three amino acids, are responsible for the formation of benzyl alcohol and its downstream derivatives, benzyl benzoate and methyl salicylate, in petunia flowers. Analysis of salicylic acid levels in petunia stems upon pathogen infection revealed that downregulation of benzaldehyde reductase expression substantially reduces salicylic acid levels. These findings provide direct evidence that benzaldehyde reductase represents the last missing enzyme in salicylic acid biosynthesis via the benzyl benzoate intermediate. Moreover, the subcellular localization of benzaldehyde reductase homologs across flowering plants is species-specific, occurring either in peroxisomes or cytosol, suggesting that different species employ distinct compartmental organization for phenylalanine-dependent salicylic acid biosynthesis.

ORGANISM(S): Cellular Organisms

SUBMITTER: Dr. Natalia Dudareva 

PROVIDER: PXD080089 | JPOST Repository | Tue Jun 23 00:00:00 BST 2026

REPOSITORIES: jPOST

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MonoQ_Anion_Exchange_Fractions_RawFiles.zip Other
MonoQ_Anion_Exchange_Fractions_Results.xlsx Xlsx
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