Nature Communications

Abstract

The plant hormone jasmonoyl-isoleucine (JA-Ile) reallocates resources from growth towards induced defenses upon microbial or herbivore attacks or other environmental threats. JA-Ile and its precursor jasmonic acid (JA) undergo complex enzymatic turnover that shape hormonal dynamics for optimal signaling. JA-Ile is inactivated through gradual oxidation by CYP94 mono-oxygenases, followed by 12-OH-JA-Ile deconjugation towards 12-OH-JA. 12-OH-JA was believed to originate also from direct JA hydroxylation by JAO/JOX dioxy-genases. Here we investigate the nature and origins of hydroxy-JAs and their derivatives upon stress responses in Arabidopsis. Using a set of analytical methods to explore enzyme assays and multiple pathway-impaired mutants, we show that JAO enzymes produce exclusively 11-OH-JA rather than 12-OH-JA and de ne a separate branch in JA catabolism. Upon leaf wounding, the CYP94/AH and, to a lesser extent, the JAO pathways direct the respective accumulation of 12- and 11-OH-JAs and their 11/12-glucosylated and 12-sulfated derivatives with isoform-speci c occurrences. In contrast, Botrytis infection triggers the exclu-sive accumulation of 11-OH-JA and 11-Glc-O-JA with complex patterns of HSO4-JA. Finally, treatment of jar1 seedlings with 11-OH-JA does not trigger transcriptional changes, reinforcing the notion that the JAO/11-OH-JA pathway represents a metabolic sink modulating JA-Ile formation. Our ndings elucidate the 11-OH-JA biosynthetic pathway and highlight stress-speci c hydroxylation signatures.

 

Reference

The 11-hydroxy-jasmonic acid pathway expands jasmonate catabolic repertoire for stress-specific hormone attenuation in Arabidopsis

Thierry Heitz, Valentin Marquis, Julie Zumsteg, Katheline Baksic, Dina Dannawi, Simon Ndecky, Dorian Schutz, Laurence Miesch, Philippe Schaeffer & Pierre Adam 

Nature Communications, Published 12 September, 2026 - DOI : https://doi.org/10.1038/s41467-026-77608-8

 

Contacts

Laurence Miesch, team SOPhy, Institut de Chimie de Strasbourg, UMR 7177.

Pierre Adam, team Biogéochimie Moléculaire, Institut de Chimie de Strasbourg, UMR 7177.

 

 

Université de Strasbourg
Centre national de la recherche scientifique | CNRS
Fondation Jean-Marie Lehn