title: A serine carboxypeptidase-like acyltransferase is required for synthesis of antimicrobial compounds and disease resistance in oats.
abstract: Serine carboxypeptidase-like (SCPL) proteins have recently emerged as a new group of plant acyltransferases. These enzymes share homology with peptidases but lack protease activity and instead are able to acylate natural products. Several SCPL acyltransferases have been characterized to date from dicots, including an enzyme required for the synthesis of glucose polyesters that may contribute to insect resistance in wild tomato (Solanum pennellii) and enzymes required for the synthesis of sinapate esters associated with UV protection in Arabidopsis thaliana. In our earlier genetic analysis, we identified the Saponin-deficient 7 (Sad7) locus as being required for the synthesis of antimicrobial triterpene glycosides (avenacins) and for broad-spectrum disease resistance in diploid oat (Avena strigosa). Here, we report on the cloning of Sad7 and show that this gene encodes a functional SCPL acyltransferase, SCPL1, that is able to catalyze the synthesis of both N-methyl anthraniloyl- and benzoyl-derivatized forms of avenacin. Sad7 forms part of an operon-like gene cluster for avenacin synthesis. Oat SCPL1 (SAD7) is the founder member of a subfamily of monocot-specific SCPL proteins that includes predicted proteins from rice (Oryza sativa) and other grasses with potential roles in secondary metabolism and plant defense.
authors.affiliation: John Ines Centre, Norwich NR4 7UH, United Kingdom.
authors.forename: Sam T
authors.initials: ST
authors.lastname: Mugford
authors.forename: Xiaoquan
authors.initials: X
authors.lastname: Qi
authors.forename: Saleha
authors.initials: S
authors.lastname: Bakht
authors.forename: Lionel
authors.initials: L
authors.lastname: Hill
authors.forename: Eva
authors.initials: E
authors.lastname: Wegel
authors.forename: Richard K
authors.initials: RK
authors.lastname: Hughes
authors.forename: Kalliopi
authors.initials: K
authors.lastname: Papadopoulou
authors.forename: Rachel
authors.initials: R
authors.lastname: Melton
authors.forename: Mark
authors.initials: M
authors.lastname: Philo
authors.forename: Frank
authors.initials: F
authors.lastname: Sainsbury
authors.forename: George P
authors.initials: GP
authors.lastname: Lomonossoff
authors.forename: Abhijeet Deb
authors.initials: AD
authors.lastname: Roy
authors.forename: Rebecca J M
authors.initials: RJ
authors.lastname: Goss
authors.forename: Anne
authors.initials: A
authors.lastname: Osbourn
mesh_terms: D000217:Acyltransferases / Q000737:chemistry / Q000145:classification / Q000235:genetics / Q000502:physiology*; D000595:Amino Acid Sequence; D000890:Anti-Infective Agents / Q000378:metabolism*; D018554:Avena / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism*; D002268:Carboxypeptidases / Q000737:chemistry / Q000145:classification / Q000235:genetics / Q000502:physiology*; D007113:Immunity, Innate / Q000235:genetics / Q000502:physiology*; D015151:Immunoblotting; D008969:Molecular Sequence Data; D010802:Phylogeny; D010940:Plant Proteins / Q000737:chemistry / Q000145:classification / Q000235:genetics / Q000502:physiology*; D055503:Protein Multimerization; D017386:Sequence Homology, Amino Acid
chemical_list: D000890:Anti-Infective Agents; D010940:Plant Proteins; D000217:Acyltransferases; D002268:Carboxypeptidases; C022633:serine carboxypeptidase
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