Degradation of salicylic acid to catechol in Solanaceae by SA 1-hydroxylase. Issue 3 (6th January 2021)

• Record Type: Journal Article
• Authors: Zhou, Fei; Last, Robert L; Pichersky, Eran
• Is Part Of: Plant physiology. Volume 185:Issue 3(2021)
• Page Start: 876
• Page End: 891
• Publication Date: 2021-01-06
• Subjects: Plant physiology -- Periodicals; Botany -- Periodicals; Periodicals; Electronic journals; 571.2
• DOI: 10.1093/plphys/kiaa096
• Languages: English
• ISSNs: 0032-0889

Abstract

Abstract: The hormone salicylic acid (SA) plays crucial roles in plant defense, stress responses, and in the regulation of plant growth and development. Whereas the biosynthetic pathways and biological functions of SA have been extensively studied, SA catabolism is less well understood. In this study, we report the identification and functional characterization of an FAD/NADH-dependent SA 1-hydroxylase from tomato ( Solanum lycopersicum ; SlSA1H), which catalyzes the oxidative decarboxylation of SA to catechol. Transcript levels of SlSA1H were highest in stems and its expression was correlated with the formation of the methylated catechol derivatives guaiacol and veratrole. Consistent with a role in SA catabolism, SlSA1H RNAi plants accumulated lower amounts of guaiacol and failed to produce any veratrole. Two O -methyltransferases involved in the conversion of catechol to guaiacol and guaiacol to veratrole were also functionally characterized. Subcellular localization analyses revealed the cytosolic localization of this degradation pathway. Phylogenetic analysis and functional characterization of SA1H homologs from other species indicated that this type of FAD/NADH-dependent SA 1-hydroxylases evolved recently within the Solanaceae family. Abstract : FAD/NADH-dependent salicylic acid 1-hydroxylases from Solanaceous species catalyze the oxidative decarboxylation of salicylic acid to catechol.