Triazine probes target ascorbate peroxidases in plants

Kyoko Morimoto, Kyle S. Cole, Jiorgos Kourelis, Collin H. Witt, Daniel Brown, Daniel Krahn, Monika Stegmann, Farnusch Kaschani, Markus Kaiser, Jonathan Burton, Shabaz Mohammed, Kazuko Yamaguchi-Shinozaki, Eranthie Weerapana, Renier A. L. van der Hoorn

Research output: Contribution to journalArticlepeer-review

5 Citations (Scopus)


Though they are rare in nature, anthropogenic 1,3,5-triazines have been used in herbicides as chemically stable scaffolds. Here, we show that small 1,3,5-triazines selectively target ascorbate peroxidases (APXs) in Arabidopsis (Arabidopsis thaliana), tomato (Solanum lycopersicum), rice (Oryza sativa), maize (Zea mays), liverwort (Marchantia polymorpha), and other plant species. The alkyne-tagged 2-chloro-4-methyl-1,3,5-triazine probe KSC-3 selectively binds APX enzymes, both in crude extracts and in living cells. KSC-3 blocks APX activity, thereby reducing photosynthetic activity under moderate light stress, even in apx1 mutant plants. This suggests that APX enzymes in addition to APX1 protect the photosystem against reactive oxygen species. Profiling APX1 with KCS-3 revealed that the catabolic products of atrazine (a 1,3,5-triazine herbicide), which are common soil pollutants, also target APX1. Thus, KSC-3 is a powerful chemical probe to study APX enzymes in the plant kingdom.

Original languageEnglish
Pages (from-to)1848-1859
Number of pages12
JournalPlant Physiology
Issue number4
Early online date28 May 2019
Publication statusPublished - Aug 2019

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