Glycosyltransferases from oat (Avena) implicated in the acylation of avenacins

Owatworakit, Amorn, Townsend, Belinda, Louveau, Thomas, Jenner, Helen, Rejzek, Martin, Hughes, Richard K., Saalbach, Gerhard, Qi, Xiaoquan, Bakht, Saleha, Roy, Abhijeet Deb, Mugford, Sam T., Goss, Rebecca J. M., Field, Robert A. ORCID: https://orcid.org/0000-0001-8574-0275 and Osbourn, Anne (2013) Glycosyltransferases from oat (Avena) implicated in the acylation of avenacins. Journal of Biological Chemistry, 288 (6). pp. 3696-3704. ISSN 0021-9258

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Abstract

Plants produce a huge array of specialized metabolites that have important functions in defense against biotic and abiotic stresses. Many of these compounds are glycosylated by family 1 glycosyltransferases (GTs). Oats (Avena spp.) make root-derived antimicrobial triterpenes (avenacins) that provide protection against soil-borne diseases. The ability to synthesize avenacins has evolved since the divergence of oats from other cereals and grasses. The major avenacin, A-l, is acylated with JV-methylanthranilic acid. Previously, we have cloned and characterized three genes for avenacin synthesis (for the triterpene synthase SAD1, a triterpene-modifying cytochrome P450 SAD2, and the serine carboxypeptidase-like acyl transferase SAD7), which form part of a biosyn the tic gene cluster. Here, we identify a fourth member of this gene cluster encoding a GT belonging to clade L of family 1 (UGT74H5), and show that this enzyme is an JV-methylanthranilic acid O-glucosyltransferase implicated in the synthesis of avenacin A-l. Two other closely related family 1 GTs (UGT74H6 and UGT74H7) are also expressed in oat roots. One of these (UGT74H6) is able to glu-cosylate both JV-methylanthranilic acid and benzoic acid, whereas the function of the other (UGT74H7) remains unknown. Our investigations indicate that UGT74H5 is likely to be key for the generation of the activated acyl donor used by SAD7 in the synthesis of the major avenacin, A-l, whereas UGT74H6 may contribute to the synthesis of other forms of avenacin that are acylated with benzoic acid.

Item Type: Article
Uncontrolled Keywords: biochemistry,molecular biology,cell biology ,/dk/atira/pure/subjectarea/asjc/1300/1303
Faculty \ School: Faculty of Science

Faculty of Science > School of Chemistry, Pharmacy and Pharmacology
Faculty of Science > School of Biological Sciences
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Depositing User: LivePure Connector
Date Deposited: 04 Sep 2024 13:36
Last Modified: 25 Sep 2024 18:06
URI: https://ueaeprints.uea.ac.uk/id/eprint/96550
DOI: 10.1074/jbc.M112.426155

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