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Plant Cell, Vol. 12, 1295-1306, August 2000, Copyright © 2000, American Society of Plant Physiologists
Cloning of the SNG1 Gene of Arabidopsis Reveals a Role for a Serine Carboxypeptidase-like Protein as an Acyltransferase in Secondary Metabolism
Claus Lehfeldta,
Amber M. Shirleyb,
Knut Meyerc,
Max O. Rueggerb,
Joanne C. Cusumanob,
Paul V. Viitanenc,
Dieter Stracka, and
Clint Chappleb
a Leibniz-Institut für Pflanzenbiochemie, Halle (Saale), Germany
b Department of Biochemistry, Purdue University, West Lafayette, Indiana 47907
c DuPont Central Research and Development, Biochemical Sciences and Engineering, Experimental Station, P.O. Box 80328, Wilmington, Delaware 19880-0328
Correspondence to:
Clint Chapple, chapple{at}purdue.edu (E-mail), 765-496-7213 (fax)
Serine carboxypeptidases contain a conserved catalytic triad of serine, histidine, and aspartic acid active-site residues. These enzymes cleave the peptide bond between the penultimate and C-terminal amino acid residues of their protein or peptide substrates. The Arabidopsis Genome Initiative has revealed that the Arabidopsis genome encodes numerous proteins with homology to serine carboxypeptidases. Although many of these proteins may be involved in protein turnover or processing, the role of virtually all of these serine carboxypeptidase-like (SCPL) proteins in plant metabolism is unknown. We previously identified an Arabidopsis mutant, sng1 (sinapoylglucose accumulator 1), that is defective in synthesis of sinapoylmalate, one of the major phenylpropanoid secondary metabolites accumulated by Arabidopsis and some other members of the Brassicaceae. We have cloned the gene that is defective in sng1 and have found that it encodes a SCPL protein. Expression of SNG1 in Escherichia coli demonstrates that it encodes sinapoylglucose:malate sinapoyltransferase, an enzyme that catalyzes a transesterification instead of functioning like a hydrolase, as do the other carboxypeptidases. This finding suggests that SCPL proteins have acquired novel functions in plant metabolism and provides an insight into the evolution of secondary metabolic pathways in plants.
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