Skip Navigation


JXB Advance Access originally published online on July 2, 2004
Journal of Experimental Botany 2004 55(404):1809-1820; doi:10.1093/jxb/erh183
This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow All Versions of this Article:
55/404/1809    most recent
erh183v1
Right arrow E-letters: Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when E-letters are posted
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 ISI Web of Science
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
Right arrow Search for citing articles in:
ISI Web of Science (11)
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Klein, M.
Right arrow Articles by Papenbrock, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Klein, M.
Right arrow Articles by Papenbrock, J.
Agricola
Right arrow Articles by Klein, M.
Right arrow Articles by Papenbrock, J.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Journal of Experimental Botany, Vol. 55, No. 404, © Society for Experimental Biology 2004; all rights reserved

RESEARCH PAPER

The multi-protein family of Arabidopsis sulphotransferases and their relatives in other plant species

Marion Klein and Jutta Papenbrock*

Institute for Botany, University of Hannover, Herrenhäuserstr. 2, D-30419 Hannover, Germany

* To whom correspondence should be addressed. Fax: +49 511 762 3992. Jutta.Papenbrock{at}botanik.uni-hannover.de

All members of the sulphotransferase (SOT, EC 2.8.2.-) protein family use 3'-phosphoadenosine 5'-phosphosulphate (PAPS) as the sulphuryl donor and transfer the sulphonate group to an appropriate hydroxyl group of several classes of substrates. These enzymes have highly conserved domains and can be found in eubacteria and eukaryotes. In mammals, sulphate conjugation catalysed by SOTs constitutes an important reaction in the transformation of xenobiotics, and in the modulation of the biological activity of steroid hormones and neurotransmitters. In plants, sulphate-conjugation reactions seem to play an important role in plant growth, development, and adaptation to stress. To date only a few plant SOTs have been characterized in detail. The flavonol 3- and 4'-SOTs from Flaveria species (Asteraceae), which catalyse the sulphonation of flavonol aglycones and flavonol 3-sulphates, respectively, were the first plant SOTs for which cDNA clones were isolated. The plasma membrane associated gallic acid SOT of Mimosa pudica L. pulvini cells may be intrinsic to signalling events that modify the seismonastic response. In Brassica napus L. a SOT catalyses the O-sulphonation of brassinosteroids and thereby abolishes specifically the biological activity of 24-epibrassinolide. The fully sequenced genome of Arabidopsis thaliana Heynh. contains in total 18 genes that are likely to encode SOT proteins based on sequence similarities of the translated products with an average identity of 51.1%. So far only one SOT from A. thaliana (At5g07000) was functionally characterized: the protein was shown to catalyse the sulphonation of 12-hydroxyjasmonate and thereby inactivate excess jasmonic acid in plants. The substrates and, therefore, the physiological roles of SOTs are very diverse. By using the numerous informative databases and methods available for the model plant A. thaliana, the elucidation of the functional role of the SOT protein family will be accelerated.

Key words: Brassica napus, Flaveria species, functional analysis, intracellular localization, substrate


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Plant CellHome page
S. G. Mugford, N. Yoshimoto, M. Reichelt, M. Wirtz, L. Hill, S. T. Mugford, Y. Nakazato, M. Noji, H. Takahashi, R. Kramell, et al.
Disruption of Adenosine-5'-Phosphosulfate Kinase in Arabidopsis Reduces Levels of Sulfated Secondary Metabolites
PLANT CELL, March 1, 2009; 21(3): 910 - 927.
[Abstract] [Full Text] [PDF]

Home page
 Plant Cell PhysiolHome page
Y. Manabe, N. Tinker, A. Colville, and B. Miki
CSR1, the Sole Target of Imidazolinone Herbicide in Arabidopsis thaliana
Plant Cell Physiol., September 1, 2007; 48(9): 1340 - 1358.
[Abstract] [Full Text] [PDF]

Home page
 ANN BOT (LOND)Home page
S. KOPRIVA
Regulation of Sulfate Assimilation in Arabidopsis and Beyond
Ann. Bot., April 1, 2006; 97(4): 479 - 495.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Y. Hirai, M. Klein, Y. Fujikawa, M. Yano, D. B. Goodenowe, Y. Yamazaki, S. Kanaya, Y. Nakamura, M. Kitayama, H. Suzuki, et al.
Elucidation of Gene-to-Gene and Metabolite-to-Gene Networks in Arabidopsis by Integration of Metabolomics and Transcriptomics
J. Biol. Chem., July 8, 2005; 280(27): 25590 - 25595.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Piotrowski, A. Schemenewitz, A. Lopukhina, A. Muller, T. Janowitz, E. W. Weiler, and C. Oecking
Desulfoglucosinolate Sulfotransferases from Arabidopsis thaliana Catalyze the Final Step in the Biosynthesis of the Glucosinolate Core Structure
J. Biol. Chem., December 3, 2004; 279(49): 50717 - 50725.
[Abstract] [Full Text] [PDF]


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.