RT Journal Article SR Electronic T1 PBS3 is the missing link in plant-specific isochorismate-derived salicylic acid biosynthesis JF bioRxiv FD Cold Spring Harbor Laboratory SP 600692 DO 10.1101/600692 A1 Dmitrij Rekhter A1 Daniel Lüdke A1 Yuli Ding A1 Kirstin Feussner A1 Krzysztof Zienkiewicz A1 Volker Lipka A1 Marcel Wiermer A1 Yuelin Zhang A1 Ivo Feussner YR 2019 UL http://biorxiv.org/content/early/2019/04/19/600692.abstract AB The phytohormone salicylic acid (SA) is a central regulator of plant immunity. Despite such functional importance, our knowledge of its biosynthesis is incomplete. Previous work showed that SA is synthesized from chorismic acid in plastids. The bulk of pathogen-induced SA derives from isochorismate generated by the catalytic activity of ISOCHORISMATE SYNTHASE1 (ICS1). How and in which cellular compartment isochorismate is converted to SA is unknown. Here we show that the pathway downstream of isochorismate requires only two additional proteins: the plastidial isochorismate exporter ENHANCED DISEASE SUSCEPTIBILITY5 (EDS5) and the cytosolic amido-transferase AvrPphB SUSCEPTIBLE3 (PBS3). PBS3 catalyzes the conjugation of glutamate to isochorismate. The reaction product isochorismate-9-glutamate spontaneously decomposes into enolpyruvyl-N-glutamate and SA. This previously unknown reaction mechanism appears to be conserved throughout the plant kingdom.One Sentence Summary Salicylic acid is synthesized via isochorismate-9-glutamate by PBS3.