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First published online May 20, 2005; 10.1104/pp.104.057950

Plant Physiology 138:1136-1148 (2005)
© 2005 American Society of Plant Biologists

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GENETICS, GENOMICS, AND MOLECULAR EVOLUTION

An Expression and Bioinformatics Analysis of the Arabidopsis Serine Carboxypeptidase-Like Gene Family1,[w]

Christopher M. Fraser, Lance W. Rider2 and Clint Chapple*

Department of Biochemistry, Purdue University, West Lafayette, Indiana 47907

The Arabidopsis (Arabidopsis thaliana) genome encodes a family of 51 proteins that are homologous to known serine carboxypeptidases. Based on their sequences, these serine carboxypeptidase-like (SCPL) proteins can be divided into several major clades. The first group consists of 21 proteins which, despite the function implied by their annotation, includes two that have been shown to function as acyltransferases in plant secondary metabolism: sinapoylglucose:malate sinapoyltransferase and sinapoylglucose:choline sinapoyltransferase. A second group comprises 25 SCPL proteins whose biochemical functions have not been clearly defined. Genes encoding representatives from both of these clades can be found in many plants, but have not yet been identified in other phyla. In contrast, the remaining SCPL proteins include five members that are similar to serine carboxypeptidases from a variety of organisms, including fungi and animals. Reverse transcription PCR results suggest that some SCPL genes are expressed in a highly tissue-specific fashion, whereas others are transcribed in a wide range of tissue types. Taken together, these data suggest that the Arabidopsis SCPL gene family encodes a diverse group of enzymes whose functions are likely to extend beyond protein degradation and processing to include activities such as the production of secondary metabolites.


1 This work was supported by the National Science Foundation (grant to C.C.) and by Purdue University (graduate fellowships to C.M.F.). This is journal paper number 2005–17562 from the Purdue University Agricultural Experiment Station.

2 Present address: Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109.

[w] The online version of this article contains Web-only data.

Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.104.057950.

* Corresponding author; e-mail chapple{at}purdue.edu; fax 765–496–7213.

Received December 9, 2004; returned for revision February 3, 2005; accepted February 11, 2005.




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