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Plant and Cell Physiology Advance Access originally published online on June 3, 2009
Plant and Cell Physiology 2009 50(7):1181-1190; doi:10.1093/pcp/pcp079
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© The Author 2009. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved.
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and the Japanese Society of Plant Physiologists are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions@oxfordjournals.org

This article appears in the following Plant and Cell Physiology issue: Special Issue Articles: Omics and Bioinformatics [View the issue table of contents]

Special Issue - Regular Paper

Omics-Based Approaches to Methionine Side Chain Elongation in Arabidopsis: Characterization of the Genes Encoding Methylthioalkylmalate Isomerase and Methylthioalkylmalate Dehydrogenase

Yuji Sawada1,2, Ayuko Kuwahara1,2, Mutsumi Nagano1,2, Tomoko Narisawa1, Akane Sakata1, Kazuki Saito1,3 and Masami Yokota Hirai1,2,*

1RIKEN Plant Science Center, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa, 230-0045 Japan
2JST, CREST, 4-1-8 Hon-chou, Kawaguchi, Saitama, 332-0012 Japan
3Graduate School of Pharmaceutical Sciences, Chiba University, 1-33 Yayoi-cho, Inage-ku, Chiba, Chiba, 263-8522 Japan

*Corresponding author: E-mail, myhirai@psc.riken.jp; Fax, +81-45-503-9489.


  Abstract

Glucosinolates (GSLs) are secondary metabolites in Brassicaceae plants synthesized from amino acids. Methionine-derived GSLs (Met-GSLs) with diverse side chains of various lengths are the major GSLs in Arabidopsis. Methionine chain elongation enzymes are responsible for variations in chain length in Met-GSL biosynthesis. The genes encoding methionine chain elongation enzymes are considered to have been recruited from the leucine biosynthetic pathway in the course of evolution. Among them, the genes encoding methylthioalkylmalate synthases and aminotransferases have been identified; however, the remaining genes that encode methylthioalkylmalate isomerase (MAM-I) and methylthioalkylmalate dehydro-genase (MAM-D) remain to be identified. In a previous study based on transcriptome co-expression analysis, we identified candidate genes for the large subunit of MAM-I and MAM-D. In this study, we confirmed their predicted functions by targeted GSL analysis of the knockout mutants, and named the respective genes MAM-IL1/AtleuC1 and MAM-D1/AtIMD1. Metabolic profiling of the knockout mutants of methionine chain elongation enzymes, conducted by means of widely targeted metabolomics, implied that these enzymes have roles in controlling metabolism from methionine to primary and methionine-related secondary metabolites. As shown here, an omics-based approach is an efficient strategy for the functional elucidation of genes involved in metabolism.

Keywords: Chain elongation - Gene function - Glucosinolate - High throughput - Methionine - Widely targeted metabolomics

Abbreviations: BCAT, branched-chain amino acid amino-transferase; GSL, glucosinolate; IPM-D, isopropylmalate dehydrogenase; IPM-IL, the large subunit of isopropylmalate isomerase; IPM-IS, the small subunit of isopropylmalate iso-merase; IPMS, isopropylmalate synthase; MAAT, methionine analog aminotransferase; MAM, methylthioalkylmalate synthase; MAM-D, methylthioalkylmalate dehydrogenase; MAM-IL, the large subunit of methylthioalkylmalate isomerase; MAM-IS, the small subunit of methylthioal-kylmalate isomerase; Met-GSL, methionine-derived glucosinolate; MS, mass spectrometry; RT–PCR, reverse transcription–PCR; UPLC, ultraperformance liquid chroma-tography.

(Received April 13, 2009; Accepted June 1, 2009)
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