The acyltransferase PMAT1 malonylates brassinolide glucoside

Sufu Gan, Wilfried Rozhon, Elisabeth Varga, Jyotirmoy Halder, Franz Berthiller, Brigitte Poppenberger

Research output: Contribution to journalArticlepeer-review

5 Scopus citations

Abstract

Brassinosteroids (BRs) are steroid hormones of plants that coordinate fundamental growth and development processes. Their homeostasis is controlled by diverse means, including glucosylation of the bioactive BR brassinolide (BL), which is catalyzed by the UDP-glycosyltransferases (UGTs) UGT73C5 and UGT73C6 and occurs mainly at the C-23 position. Addi tional evidence had suggested that the resultant BL-23-O glucoside (BL-23-O-Glc) can be malonylated, but the physio logical significance of and enzyme required for this reaction had remained unknown. Here, we show that in Arabidopsis thaliana malonylation of BL-23-O-Glc is catalyzed by the acyltransferase phenolic glucoside malonyl-Transferase 1 (PMAT1), which is also known to malonylate phenolic gluco sides and lipid amides. Loss of PMAT1 abolished BL-23-O malonylglucoside formation and enriched BL-23-O-Glc, showing that the enzyme acts on the glucoside. An over expression of PMAT1 in plants where UGT73C6 was also overexpressed, and thus, BL-23-O-Glc formation was pro moted, enhanced the symptoms of BR-deficiency of UGT73-C6oe plants, providing evidence that PMAT1 contributes to BL inactivation. Based on these results, a model is proposed in which PMAT1 acts in the conversion of both endogenous and xenobiotic glucosides to adjust metabolic homeostasis in spatial and temporal modes.

Original languageEnglish
Article number100424
JournalJournal of Biological Chemistry
Volume296
DOIs
StatePublished - 1 Jan 2021

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