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Published on June 28, 2007; 10.1104/pp.107.098970

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Received March 6, 2007
Accepted June 22, 2007

Related Arabidopsis Serine Carboxypeptidase-like Sinapoylglucose Acyltransferases Display Distinct but Overlapping Substrate Specificities

Christopher M. Fraser , Michael G. Thompson , Amber M. Shirley , John Ralph , Jessica A. Schoenherr , Taksina Sinlapadech , Mark C. Hall , and Clint Chapple *

Department of Biochemistry, Purdue University, West Lafayette, IN 47907; US Dairy Forage Research Center, USDA-Agricultural Research Service, 1925 Linden Drive West, Madison, WI 53706, USA

* Corresponding author; email: chapple{at}purdue.edu.

The Arabidopsis genome encodes fifty-one proteins annotated as serine carboxypeptidase-like (SCPL) enzymes. Nineteen of these SCPL proteins are highly similar to one another, and represent a clade that appears to be unique to plants. Two of the most divergent proteins within this group have been characterized to date, sinapoylglucose: malate sinapoyltransferase (SMT) and sinapoylglucose:choline sinapoyltransferase (SCT). The fact that two of the least related proteins within this clade are acyltransferases rather than true serine carboxypeptidases suggests that some or all of the remaining members of this group may have similar activities. The gene that encodes SMT (SNG1: At2g22990) is one of five SCPL genes arranged in a cluster on chromosome 2. In this study, an analysis of deletion mutant lines lacking one or more genes in this SCPL gene cluster reveals that three of these genes also encode sinapoylglucose-dependent acyltransferases. At2g23000 encodes sinapoylglucose: anthocyanin acyltransferase (SAT), an enzyme that is required for the synthesis of the sinapoylated anthocyanins in Arabidopsis. At2g23010 encodes an enzyme capable of synthesizing 1,2-disinapoylglucose from two molecules of sinapoylglucose, an activity shared by SNG1 and At2g22980. Sequence analysis of these SCPL proteins reveals pair-wise percent identities that range from 71% to 78%, suggesting that their differing specificities for acyl acceptor substrates are due to changes in a relatively small subset of amino acids. The study of these SCPL proteins provides an opportunity to examine enzyme structure-function relationships and may shed light on the role of evolution of hydroxycinnamate ester metabolism and the SCPL gene family in Arabidopsis and other flowering plants.




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