The sng2 mutant of Arabidopsis is defective in the gene encoding the serine carboxypeptidase-like protein sinapoylglucose : choline sinapoyltransferase
Am. Shirley et al., The sng2 mutant of Arabidopsis is defective in the gene encoding the serine carboxypeptidase-like protein sinapoylglucose : choline sinapoyltransferase, PLANT J, 28(1), 2001, pp. 83-94
Serine carboxypeptidase-like (SCPL) proteins have traditionally been assign
ed roles in the hydrolytic processing of proteins; however, several SCPL pr
oteins have recently been identified as catalysts in transacylation reactio
ns of plant secondary metabolism. The novel functions of these enzymes sugg
est a catalytic diversity for plant SCPL proteins that extends beyond simpl
e hydrolysis reactions. Characterization of the Arabidopsis sng2 (sinapoylg
lucose accumulator 2) mutant has identified another SCPL protein involved i
n plant secondary metabolism. The sng2 mutant was isolated by screening see
d extracts for altered levels of sinapate esters, a group of phenylpropanoi
d compounds found in Arabidopsis and some other members of the Brassicaceae
. Homozygous sng2 seeds accumulate sinapoylglucose instead of sinapoylcholi
ne, and have increased levels of choline and decreased activity of the enzy
me sinapoylglucose:choline sinapoyltransferase (SCT). Cloning of the SNG2 g
ene by a combination of map-based and candidate gene approaches demonstrate
s that SCT is another member of the growing class of SCPL acyltransferases
involved in plant secondary metabolism.