Skip Navigation


Glycobiology Advance Access originally published online on November 1, 2002
This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow All Versions of this Article:
13/3/139    most recent
cwg017v1
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 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 (31)
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Lim, E.-K.
Right arrow Articles by Bowles, D. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lim, E.-K.
Right arrow Articles by Bowles, D. J.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Glycobiology, 2003, Vol. 13, No. 3 139-145
© 2003 Oxford University Press

Evolution of substrate recognition across a multigene family of glycosyltransferases in Arabidopsis

Eng-Kiat Lim3, Sandie Baldauf4, Yi Li3, Luisa Elias3, Dawn Worrall2,3, Steven P. Spencer3, Rosamond G. Jackson3, Goro Taguchi5, Joe Ross3 and Dianna J. Bowles1,3

3 Centre for Novel Agricultural Products, Department of Biology, University of York, York YO10 5DD, United Kingdom
4 Department of Biology, University of York, York YO10 5DD, United Kingdom
5 Gene Research Center, Shinshu University, Ueda, Nagano 386-8567, Japan

Received on April 19, 2002; revised on September 24, 2002; accepted on September 24, 2002

The complete sequence of the Arabidopsis genome enables definitive characterization of multigene families and analysis of their phylogenetic relationships. Using a consensus sequence previously defined for glycosyltransferases that use small-molecular-weight acceptors, 107 gene sequences were identified in the Arabidopsis genome and used to construct a phylogenetic tree. Screening recombinant proteins for their catalytic activities in vitro has revealed enzymes active toward physiologically important substrates, including hormones and secondary metabolites. The aim of this study has been to use the phylogenetic relationships across the entire family to explore the evolution of substrate recognition and regioselectivity of glucosylation. Hydroxycoumarins have been used as the model substrates for the analysis in which 90 sequences have been assayed and 48 sequences shown to recognize these compounds. The study has revealed activity in 6 of the 14 phylogenetic groups of the multigene family, suggesting that basic features of substrate recognition are retained across substantial evolutionary periods.

2 Present address: Department of Biological Sciences, IENS, Lancaster University, Lancaster LA1 4YQ, United Kingdom

1 To whom correspondence should be addressed; e-mail:djb32{at}york.ac.uk


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
A. Noguchi, M. Horikawa, Y. Fukui, M. Fukuchi-Mizutani, A. Iuchi-Okada, M. Ishiguro, Y. Kiso, T. Nakayama, and E. Ono
Local Differentiation of Sugar Donor Specificity of Flavonoid Glycosyltransferase in Lamiales
PLANT CELL, May 1, 2009; 21(5): 1556 - 1572.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
S. A. Osmani, S. Bak, A. Imberty, C. E. Olsen, and B. L. Moller
Catalytic Key Amino Acids and UDP-Sugar Donor Specificity of a Plant Glucuronosyltransferase, UGT94B1: Molecular Modeling Substantiated by Site-Specific Mutagenesis and Biochemical Analyses
Plant Physiology, November 1, 2008; 148(3): 1295 - 1308.
[Abstract] [Full Text] [PDF]

Home page
 J Exp BotHome page
M. Griesser, F. Vitzthum, B. Fink, M. L. Bellido, C. Raasch, J. Munoz-Blanco, and W. Schwab
Multi-substrate flavonol O-glucosyltransferases from strawberry (Fragariaxananassa) achene and receptacle
J. Exp. Bot., July 1, 2008; 59(10): 2611 - 2625.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. M. Cartwright, E.-K. Lim, C. Kleanthous, and D. J. Bowles
A Kinetic Analysis of Regiospecific Glucosylation by Two Glycosyltransferases of Arabidopsis thaliana: DOMAIN SWAPPING TO INTRODUCE NEW ACTIVITIES
J. Biol. Chem., June 6, 2008; 283(23): 15724 - 15731.
[Abstract] [Full Text] [PDF]

Home page
 J Exp BotHome page
S. Dhaubhadel, M. Farhangkhoee, and R. Chapman
Identification and characterization of isoflavonoid specific glycosyltransferase and malonyltransferase from soybean seeds
J. Exp. Bot., March 2, 2008; (2008) ern046v2.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
M. Brazier-Hicks, W. A. Offen, M. C. Gershater, T. J. Revett, E.-K. Lim, D. J. Bowles, G. J. Davies, and R. Edwards
Characterization and engineering of the bifunctional N- and O-glucosyltransferase involved in xenobiotic metabolism in plants
PNAS, December 18, 2007; 104(51): 20238 - 20243.
[Abstract] [Full Text] [PDF]

Home page
 Appl. Environ. Microbiol.Home page
B. Poppenberger, F. Berthiller, H. Bachmann, D. Lucyshyn, C. Peterbauer, R. Mitterbauer, R. Schuhmacher, R. Krska, J. Glossl, and G. Adam
Heterologous Expression of Arabidopsis UDP-Glucosyltransferases in Saccharomyces cerevisiae for Production of Zearalenone-4-O-Glucoside.
Appl. Envir. Microbiol., June 1, 2006; 72(6): 4404 - 4410.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
H. Shao, X. He, L. Achnine, J. W. Blount, R. A. Dixon, and X. Wang
Crystal Structures of a Multifunctional Triterpene/Flavonoid Glycosyltransferase from Medicago truncatula
PLANT CELL, November 1, 2005; 17(11): 3141 - 3154.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
K. S. Thorsoe, S. Bak, C. E. Olsen, A. Imberty, C. Breton, and B. Lindberg Moller
Determination of Catalytic Key Amino Acids and UDP Sugar Donor Specificity of the Cyanohydrin Glycosyltransferase UGT85B1 from Sorghum bicolor. Molecular Modeling Substantiated by Site-Specific Mutagenesis and Biochemical Analyses
Plant Physiology, October 1, 2005; 139(2): 664 - 673.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. R. Baerson, A. Sanchez-Moreiras, N. Pedrol-Bonjoch, M. Schulz, I. A. Kagan, A. K. Agarwal, M. J. Reigosa, and S. O. Duke
Detoxification and Transcriptome Response in Arabidopsis Seedlings Exposed to the Allelochemical Benzoxazolin-2(3H)-one
J. Biol. Chem., June 10, 2005; 280(23): 21867 - 21881.
[Abstract] [Full Text] [PDF]

Home page
 Plant Cell PhysiolHome page
N. Sasaki, K. Wada, T. Koda, K. Kasahara, T. Adachi, and Y. Ozeki
Isolation and Characterization of cDNAs Encoding an Enzyme with Glucosyltransferase Activity for cyclo-DOPA from Four O'clocks and Feather Cockscombs
Plant Cell Physiol., April 1, 2005; 46(4): 666 - 670.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
B. Hou, E.-K. Lim, G. S. Higgins, and D. J. Bowles
N-Glucosylation of Cytokinins by Glycosyltransferases of Arabidopsis thaliana
J. Biol. Chem., November 12, 2004; 279(46): 47822 - 47832.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
B. Poppenberger, F. Berthiller, D. Lucyshyn, T. Sieberer, R. Schuhmacher, R. Krska, K. Kuchler, J. Glossl, C. Luschnig, and G. Adam
Detoxification of the Fusarium Mycotoxin Deoxynivalenol by a UDP-glucosyltransferase from Arabidopsis thaliana
J. Biol. Chem., November 28, 2003; 278(48): 47905 - 47914.
[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.