Skip Navigation



JXB Advance Access published online on June 23, 2006
Journal of Experimental Botany, doi:10.1093/jxb/erj205
This Article
Right arrow FREE Full Text (PDF) Freely available
Right arrow All Versions of this Article:
57/10/2339    most recent
erj205v1
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 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 arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Minic, Z.
Right arrow Articles by Jouanin, L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Minic, Z.
Right arrow Articles by Jouanin, L.
Agricola
Right arrow Articles by Minic, Z.
Right arrow Articles by Jouanin, L.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Published by Oxford University Press [2006] on behalf of the Society for Experimental Biology.
Received December 23, 2005
Accepted March 16, 2006

RESEARCH PAPER

Purification, functional characterization, cloning, and identification of mutants of a seed-specific arabinan hydrolase in Arabidopsis

Zoran Minic 1, Cao-Trung Do 1, Christophe Rihouey 2, Halima Morin 1, Patrice Lerouge 2, and Lise Jouanin 1 *

1 Laboratoire de Biologie Cellulaire - Institut National de la Recherche Agronomique, Route de St-Cyr, F-78026 Versailles Cedex, France
2 Faculté des Sciences, UMR 6037 CNRS, IFRMP23, Université de Rouen, F-76821 Mont Saint Aignan Cedex, France

* To whom correspondence should be addressed.
Lise Jouanin, E-mail: jouanin{at}versailles.inra.fr


  Abstract

This work describes the purification and characterization of an enzyme that exhibits arabinan hydrolase activity in seeds of Arabidopsis thaliana. The enzyme, designated XYL3, had an apparent molecular mass of 80 kDa when purified to homogeneity, and was identified using MALDI-TOF (matrix-assisted laser desorption ionization-time of flight) as a putative {beta}-D-xylosidase that belongs to family 3 of glycoside hydrolases encoded by gene At5g09730. XYL3 hydrolysed synthetic substrates such as p-nitrophenyl-{alpha}-L-arabinofuranoside and p-nitrophenyl-{beta}-D-xyloside with similar catalytic efficiency. XYL3 released L-arabinose from (1->5)-{alpha}-L-arabinofuranobiose, arabinoxylan, sugar beet arabinan, and debranched arabinan. The enzyme hydrolysed both arabinosyl-substituted side group residues and terminal arabinofuranosyl residues (1->5)-{alpha}-linked to the arabinan backbone. This indicates that XYL3 is able to degrade all terminal arabinosyl residues and suggests that it participates in the in-vivo hydrolysis of arabinan. Analysis of gene expression patterns by semi-quantitative RT-PCR, in-situ hybridization and a promoter-GUS fusion demonstrated that AtBX3 was specifically expressed in the seed endosperm at the globular stage of the embryo. Immunolocalization using LM6 anti-arabinan antisera found that arabinan, the XYL3 substrate, was also present in this seed tissue. T-DNA null mutants for AtBX3 were identified. The mutant plants lacked the {alpha}-L-arabinofuranosidase and {beta}-D-xylosidase activities corresponding to XYL3. Mutants showed reduced seed size and are delayed in seedling germination compared with the wild type.

Keywords: Arabidopsis thaliana; arabinan; {alpha}-L-arabinofuranosidase; cell wall; endosperm; seed.
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
 Mol PlantHome page
L. D. Gomez, C. G. Steele-King, L. Jones, J. M. Foster, S. Vuttipongchaikij, and S. J. McQueen-Mason
Arabinan Metabolism during Seed Development and Germination in Arabidopsis
Mol Plant, September 1, 2009; 2(5): 966 - 976.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
A. A. Arsovski, T. M. Popma, G. W. Haughn, N. C. Carpita, M. C. McCann, and T. L. Western
AtBXL1 Encodes a Bifunctional {beta}-D-Xylosidase/{alpha}-L-Arabinofuranosidase Required for Pectic Arabinan Modification in Arabidopsis Mucilage Secretory Cells
Plant Physiology, July 1, 2009; 150(3): 1219 - 1234.
[Abstract] [Full Text] [PDF]

Home page
 Plant Cell PhysiolHome page
A. Eudes, G. Mouille, J. Thevenin, A. Goyallon, Z. Minic, and L. Jouanin
Purification, Cloning and Functional Characterization of an Endogenous beta-Glucuronidase in Arabidopsis thaliana
Plant Cell Physiol., September 1, 2008; 49(9): 1331 - 1341.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
R. A. Chavez Montes, P. Ranocha, Y. Martinez, Z. Minic, L. Jouanin, M. Marquis, L. Saulnier, L. M. Fulton, C. S. Cobbett, F. Bitton, et al.
Cell Wall Modifications in Arabidopsis Plants with Altered {alpha}-L-Arabinofuranosidase Activity
Plant Physiology, May 1, 2008; 147(1): 63 - 77.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
A. Macquet, M.-C. Ralet, O. Loudet, J. Kronenberger, G. Mouille, A. Marion-Poll, and H. M. North
A Naturally Occurring Mutation in an Arabidopsis Accession Affects a {beta}-D-Galactosidase That Increases the Hydrophilic Potential of Rhamnogalacturonan I in Seed Mucilage
PLANT CELL, December 1, 2007; 19(12): 3990 - 4006.
[Abstract] [Full Text] [PDF]

Home page
 J Exp BotHome page
J.-S. Xiong, M. Balland-Vanney, Z.-P. Xie, M. Schultze, A. Kondorosi, E. Kondorosi, and C. Staehelin
Molecular cloning of a bifunctional -xylosidase/{alpha}-L-arabinosidase from alfalfa roots: heterologous expression in Medicago truncatula and substrate specificity of the purified enzyme
J. Exp. Bot., August 1, 2007; 58(11): 2799 - 2810.
[Abstract] [Full Text] [PDF]

Home page
 J Exp BotHome page
Z. Minic, E. Jamet, L. Negroni, P Arsene der Garabedian, M. Zivy, and L. Jouanin
A sub-proteome of Arabidopsis thaliana mature stems trapped on Concanavalin A is enriched in cell wall glycoside hydrolases
J. Exp. Bot., July 1, 2007; 58(10): 2503 - 2512.
[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.