Plant Physiol. Illumina
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

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

OPEN ACCESS ARTICLE
This Article
Free via Open Access: OA
Right arrow Full Text (Plant Physiology Preview (PDF))
Right arrowOA All Versions of this Article:
144/4/1986    most recent
pp.107.098970v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Web of Science (13)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Fraser, C. M.
Right arrow Articles by Chapple, C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Fraser, C. M.
Right arrow Articles by Chapple, C.
Agricola
Right arrow Articles by Fraser, C. M.
Right arrow Articles by Chapple, C.

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.




This article has been cited by other articles:


Home page
 Mol PlantHome page
X. Li, J. Bergelson, and C. Chapple
The ARABIDOPSIS Accession Pna-10 Is a Naturally Occurring sng1 Deletion Mutant
Mol Plant, November 10, 2009; (2009) ssp090v1.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
S. T. Mugford, X. Qi, S. Bakht, L. Hill, E. Wegel, R. K. Hughes, K. Papadopoulou, R. Melton, M. Philo, F. Sainsbury, et al.
A Serine Carboxypeptidase-Like Acyltransferase Is Required for Synthesis of Antimicrobial Compounds and Disease Resistance in Oats
PLANT CELL, August 1, 2009; 21(8): 2473 - 2484.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
K. Yonekura-Sakakibara, T. Tohge, F. Matsuda, R. Nakabayashi, H. Takayama, R. Niida, A. Watanabe-Takahashi, E. Inoue, and K. Saito
Comprehensive Flavonol Profiling and Transcriptome Coexpression Analysis Leading to Decoding Gene-Metabolite Correlations in Arabidopsis
PLANT CELL, August 1, 2008; 20(8): 2160 - 2176.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
C. Bottcher, E. von Roepenack-Lahaye, J. Schmidt, C. Schmotz, S. Neumann, D. Scheel, and S. Clemens
Metabolome Analysis of Biosynthetic Mutants Reveals a Diversity of Metabolic Changes and Allows Identification of a Large Number of New Compounds in Arabidopsis
Plant Physiology, August 1, 2008; 147(4): 2107 - 2120.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 2007 by the American Society of Plant Biologists