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

ABSTRACT: To study glycosyltransferases from oat, root proteins were extracted and separated gy 1D SDS gel electrophoresis. Bands were cut out, digested with trypsin, and the resulting peptides were analysed by LCMSMS on an Orbitrap mass sepctrometer. Raw data was processed with MaxQuant 1.3.0.5, and database searches on a custom database performed using Mascot.

INSTRUMENT(S):

ORGANISM(S): Avena Strigosa (black Oat)

SUBMITTER: Gerhard Saalbach

LAB HEAD: Gerhard Saalbach

PROVIDER: PXD000083 | Pride | 2013-04-24

REPOSITORIES: Pride

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			Action	DRS
	081208_03.RAW	Raw
	081209_01.RAW	Raw
	PRIDE_Exp_Complete_Ac_27977.pride.mgf.gz	Mgf
	PRIDE_Exp_Complete_Ac_27977.pride.mztab.gz	Mztab
	PRIDE_Exp_Complete_Ac_27977.xml.gz	Xml

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

Owatworakit Amorn A Townsend Belinda B Louveau Thomas T Jenner Helen H Rejzek Martin M Hughes Richard K RK Saalbach Gerhard G Qi Xiaoquan X Bakht Saleha S Roy Abhijeet Deb AD Mugford Sam T ST Goss Rebecca J M RJ Field Robert A RA Osbourn Anne A

The Journal of biological chemistry 20121220 6

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-1, is acylated with N-methyl ...[more]

PMID: 23258535

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

Project description: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-1, is acylated with N-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 biosynthetic 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 N-methylanthranilic acid O-glucosyltransferase implicated in the synthesis of avenacin A-1. Two other closely related family 1 GTs (UGT74H6 and UGT74H7) are also expressed in oat roots. One of these (UGT74H6) is able to glucosylate both N-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-1, whereas UGT74H6 may contribute to the synthesis of other forms of avenacin that are acylated with benzoic acid.

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