Disruption of Zea mays isochorismate synthase1 decreases PHENYLALANINE AMMONIA LYASE activity and suppresses hypersensitive response-induced metabolism
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ISOCHORISMATE SYNTHASE (ICS) catalyzes the isomerization of chorismate to isochorismate, an essential precursor in the biosynthesis of the Photosystem I electron carrier phylloquinone and of one of two pathways for the biosynthesis of the defense response hormone salicylic acid (SA). We characterized a Zea mays ics1 mutant for impacts on metabolism, photosynthesis, and immune signaling. Phylloquinone was reduced in the mutant resulting in low electron transfer rates and high electron backflow rates. SA accumulation induced by autoactive alleles of the nucleotide-binding leucine-rich repeat (NLR) gene Resistance to Puccinia sorgi1 (Rp1) required ics1. Induced accumulation of SA was not required for lesion formation by the autoactive Rp1-D21#4 allele. Metabolomic analyses and SA supplementation of Rp1-D21#4 mutants, ics1-1 mutants and Rp1-D21#4; ics1-1 double mutants demonstrated that most hypersensitive response-induced metabolism required ics1 but this was independent of SA accumulation. Both the PAL and ICS pathways contributed to SA biosynthesis in maize as labeled phenylalanine was incorporated into SA glucoside. Maize ics1-1 mutants had low PHENYLALANINE AMMONIA LYASE activity, accumulated phenylalanine, and decreased abundance of phenylalanine derived metabolites. This demonstrates that the ICS and PAL pathways interact by a yet unknown mechanism complicating the interpretation of SA biosynthesis in plants from genetics alone.
Publication Date
11-2022
Recommended Citation
McCoy, Rachel; Benke, Ryan; Ibrahim, Iskander; Simpson, Jeffery; Muro-Villanueva, Fabiola; Zahn, Ross; Chapple, Clint; Widhalm, Joshua; Puthiyaveetil, Sujith; Johal, Gurmukh; and Dilkes, Brian, "Disruption of Zea mays isochorismate synthase1 decreases PHENYLALANINE AMMONIA LYASE activity and suppresses hypersensitive response-induced metabolism" (2022). Faculty Creative and Scholarly Works. 55.
https://digitalcommons.snc.edu/faculty_staff_works/55
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