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JXB Advance Access originally published online on June 23, 2006
Journal of Experimental Botany 2006 57(10):2339-2351; doi:10.1093/jxb/erj205
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Published by Oxford University Press [2006] on behalf of the Society for Experimental Biology.

RESEARCH PAPER

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

Zoran Minic1, Cao-Trung Do1, Christophe Rihouey2, Halima Morin1, Patrice Lerouge2 and Lise Jouanin1,*

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

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

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 ß-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-ß-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 ß-D-xylosidase activities corresponding to XYL3. Mutants showed reduced seed size and are delayed in seedling germination compared with the wild type.

Key words: Arabidopsis thaliana, arabinan, {alpha}-L-arabinofuranosidase, cell wall, endosperm, seed


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