The Role of Peroxidase in Suberin Assembly in Potato
Abstract
Suberin is a complex heteropolymer that forms an apoplastic diffusion barrier in plant tissues, protecting against water loss and pathogen invasion. In potato tubers (Solanum tuberosum), suberization is a key wound-healing response that requires coordinated deposition of phenolic and aliphatic monomers. Although suberin biosynthesis has been studied extensively, the specific roles of individual class III peroxidases (PRXs) in catalyzing oxidative polymerization of phenolic monomers remain unclear. Here, we examined the functional contributions of three wound-inducible peroxidase genes—PRX19, PRX55, and PRX105—using RNA interference (RNAi) knockdown to dissect isoform-specific roles in suberin assembly and barrier formation. Transcript analyses confirmed strong (>80%) silencing of each target gene, yet physiological and biochemical consequences varied substantially. PRX19-RNAi tubers showed sharply reduced total peroxidase activity, substantial loss of phenolic suberin, disrupted lamellar ultrastructure, and impaired water-retention capacity. Metabolic profiling revealed altered accumulation of soluble phenolics and defective incorporation of aliphatic monomers, indicating that PRX19 is required to generate phenolic radicals that form the initial poly(phenolic) scaffold necessary for subsequent aliphatic deposition. By contrast, PRX55- and PRX105-RNAi lines displayed only modest or negligible effects on peroxidase activity, suberin chemistry, and barrier integrity, suggesting partial redundancy or supporting roles during wound healing. Together, these findings support a model in which PRX19 acts as a central catalytic hub in early suberin assembly, governing phenolic coupling and lamellar organization. This work advances understanding of the enzymatic and metabolic coordination underlying wound-induced suberization and highlights PRX19 as a potential molecular target for improving postharvest tuber quality, stress tolerance, and disease resistance through targeted modulation of peroxidase activity.