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Plant Physiol, June 2001, Vol. 126, pp. 910-920

Cloning and Expression Pattern of a Gene Encoding an alpha -Xylosidase Active against Xyloglucan Oligosaccharides from Arabidopsis1

Javier Sampedro, Carmen Sieiro, Gloria Revilla, Tomás González-Villa, and Ignacio Zarra*

Departamento de Biología Vegetal, Laboratorio de Fisiología Vegetal, Facultad de Biología (J.S., G.R., I.Z.) and Departamento de Microbiología y Parasitología, Laboratorio de Microbiología, Facultad de Farmacia (C.S., T.G.-V.), Universidad de Santiago de Compostela, E-15782 Santiago de Compostela, Spain

An alpha -xylosidase active against xyloglucan oligosaccharides was purified from cabbage (Brassica oleracea var. capitata) leaves. Two peptide sequences were obtained from this protein, the N-terminal and an internal one, and these were used to identify an Arabidopsis gene coding for an alpha -xylosidase that we propose to call AtXYL1. It has been mapped to a region of chromosome I between markers at 100.44 and 107.48 cM. AtXYL1 comprised three exons and encoded a peptide that was 915 amino acids long, with a potential signal peptide of 22 amino acids and eight possible N-glycosylation sites. The protein encoded by AtXYL1 showed the signature regions of family 31 glycosyl hydrolases, which comprises not only alpha -xylosidases, but also alpha -glucosidases. The alpha -xylosidase activity is present in apoplastic extractions from Arabidopsis seedlings, as suggested by the deduced signal peptide. The first eight leaves from Arabidopsis plants were harvested to analyze alpha -xylosidase activity and AtXYL1 expression levels. Both increased from older to younger leaves, where xyloglucan turnover is expected to be higher. When this gene was introduced in a suitable expression vector and used to transform Saccharomyces cerevisiae, significantly higher alpha -xylosidase activity was detected in the yeast cells. alpha -Glucosidase activity was also increased in the transformed cells, although to a lesser extent. These results show that AtXYL1 encodes for an apoplastic alpha -xylosidase active against xyloglucan oligosaccharides that probably also has activity against p-nitrophenyl-alpha -D-glucoside.

1 This work was supported by the Dirección General de Enseñanza Superior e Investigación Científica (grant no. PB98-0640) and by Xunta de Galicia (grant no. PGIDT00PXI20002PN).

* Corresponding author; e-mail bvzarra{at}usc.es; fax 34-981-596904.

© 2001 American Society of Plant Physiologists


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