The acyltransferase PMAT1 malonylates brassinolide glucoside
Autor: | Elisabeth Varga, Jyotirmoy Halder, Franz Berthiller, Brigitte Poppenberger, Wilfried Rozhon, Sufu Gan |
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Rok vydání: | 2020 |
Předmět: |
0301 basic medicine
medicine.medical_treatment BL brassinolide Arabidopsis Biochemistry chemistry.chemical_compound Glucosides Gene Expression Regulation Plant catabolic inactivation Brassinosteroid Arabidopsis thaliana BL-23-O-Glc BL-23-O-glucoside chemistry.chemical_classification biology steroid NASC Nottingham Arabidopsis Stock Center malonylTFs malonyltransferases Plants Genetically Modified ddc CS castasterone Acyltransferase Steroids lipids (amino acids peptides and proteins) Research Article CoA coenzyme A malonylation hormone macromolecular substances PMAT1 phenolic glucoside malonyl-transferase 1 Steroid 03 medical and health sciences Steroids Heterocyclic ORF open reading frame Glucoside Transferases Brassinosteroids Glycosyltransferase medicine BR-MalGlc BR malonylglucosides Molecular Biology Brassinolide BR brassinosteroid 030102 biochemistry & molecular biology Arabidopsis Proteins ACC aminocyclopropane-1-carboxylic acid Glycosyltransferases BR-Glc BR glucoside Cell Biology biology.organism_classification carbohydrates (lipids) UGT glycosyltransferase 030104 developmental biology Enzyme chemistry biology.protein Acyltransferases |
Zdroj: | The Journal of Biological Chemistry |
Popis: | 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. Additional evidence had suggested that the resultant BL-23-O-glucoside (BL-23-O-Glc) can be malonylated, but the physiological 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 glucosides 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 overexpression of PMAT1 in plants where UGT73C6 was also overexpressed, and thus, BL-23-O-Glc formation was promoted, enhanced the symptoms of BR-deficiency of UGT73C6oe 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. |
Databáze: | OpenAIRE |
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