Cloning of a Cicer arietinum β-Galactosidase with Pectin-Degrading Function

The cDNA clone (CanBGal-3) encoding a cell wall pectin- degrading  -galactosidase ( III-Gal) from Cicer arietinum L. cv. Castellana has been identified. The identification was carried out by comparing the deduced amino acid sequences of several isolated chickpea  -galactosidase clones with the purif...

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Detalles Bibliográficos
Autores: Esteban Gallego, María Rocío, Dopico, Berta, Muñoz, Francisco J., Romo, Silvia, Martín Sánchez, José Ignacio, Labrador, Emilia
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2003
País:España
Institución:Universidad de Salamanca (USAL)
Repositorio:GREDOS. Repositorio Institucional de la Universidad de Salamanca
OAI Identifier:oai:gredos.usal.es:10366/156957
Acceso en línea:http://hdl.handle.net/10366/156957
Access Level:acceso abierto
Palabra clave:Cicer arietinum
Elongation
Epicotyls
Galactosidases
Growth
Descripción
Sumario:The cDNA clone (CanBGal-3) encoding a cell wall pectin- degrading  -galactosidase ( III-Gal) from Cicer arietinum L. cv. Castellana has been identified. The identification was carried out by comparing the deduced amino acid sequences of several isolated chickpea  -galactosidase clones with the purified  III-Gal protein sequence. The expression pattern of the gene corresponding to CanBGal-3 was in concordance with the fluctuations of the enzyme  III-Gal in different seedling organs, being specific to elongating organs such as epicotyls and roots. Transformation of Solanum tuberosum plants with the chickpea CanBGal-3 clone indicated that the  -galactosidase encoded by this clone is a pectin-degrading enzyme. The authors propose an important role for chickpea  III-Gal in pectin degradation in cell walls of vegetative organs such as epicotyls and roots. The degradation of galactan carried out by this enzyme may determine structural changes and affect cell wall porosity. It is suggested that the increase in the size of cell wall pores could permit access of other cell wall-modifying enzymes to their substrate.