Skip Navigation


Plant and Cell Physiology Advance Access originally published online on July 24, 2009
Plant and Cell Physiology 2009 50(9):1579-1586; doi:10.1093/pcp/pcp110
This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow Supplementary Data
Right arrowOA All Versions of this Article:
50/9/1579    most recent
pcp110v1
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 PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Google Scholar
Right arrow Articles by Sawada, Y.
Right arrow Articles by Hirai, M. Y.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sawada, Y.
Right arrow Articles by Hirai, M. Y.
Agricola
Right arrow Articles by Sawada, Y.
Right arrow Articles by Hirai, M. Y.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 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


Rapid Paper

Arabidopsis Bile Acid:Sodium Symporter Family Protein 5 is Involved in Methionine-Derived Glucosinolate Biosynthesis

Yuji Sawada1,2, Kiminori Toyooka1, Ayuko Kuwahara1,2, Akane Sakata1, Mutsumi Nagano1,2, 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{at}psc.riken.jp; Fax, +81-45-503-9489.


   Abstract

Glucosinolates (GSLs) are a group of plant secondary metabolites that have repellent activity against herbivore insects and pathogens, and anti-carcinogenic activity in humans. They are produced in plants of the Brassicaceae and other related families. Biosynthesis of GSLs from precursor amino acids takes place in two subcellular compartments; amino acid biosynthesis and side chain elongation occur mainly in the chloroplast, whereas the following core structure synthesis takes place in the cytosol. Although the genes encoding biosynthetic enzymes of GSLs are well known in Arabidopsis thaliana, the transporter genes responsible for translocation of biosynthetic intermediates between the chloroplast and cytosol are as yet unidentified. In this study, we identified the bile acid:sodium symporter family protein 5 (BASS5) gene in Arabidopsis as a candidate transporter gene involved in methionine-derived GSL (Met-GSL) biosynthesis by means of transcriptome co-expression analysis. Knocking out BASS5 resulted in a decrease of Met-GSLs and concomitant increase of methionine. A transient assay using fluorescence fusion proteins indicated a chloroplastic localization of BASS5. These results supported the idea that BASS5 plays a role in translocation across the chloroplast membranes of the biosynthetic intermediates of Met-GSLs.

Keywords: Arabidopsis thaliana - Bile acid:sodium symporter family protein - Co-expression - Glucosinolate - Methionine chain elongation - Widely targeted metabolomics

Abbreviations: ACC, 1-aminocyclopropane-1-carboxylic acid; BASS, bile acid:sodium symporter family protein; BCAT, branched-chain aminotransferase; cTP, chloroplast transit peptide; GSL, glucosinolate; MAAT, methionine analog aminotransferase; MAM, methylthioalkylmalate synthase; MAM-D, methylthioalkylmalate dehydrogenase; MAM-IL, a large subunit of methylthioalkylmalate isomerase; MAM-IS, a small subunit of methylthioalkylmalate isomerase; Met-GSL, Met-derived glucosinolate; MS, mass spectrometry; MTA, 5'-S-methyl-5'-thioadenosine; RT–PCR, reverse transcription–PCR; SAM, S-adenosylmethionine; SMM, S-methylmethionine; UPLC, ultra performance liquid chromatography; YFP, yellow fluorescent protein.

(Received June 10, 2009; Accepted July 10, 2009)
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.