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GrainGenes Reference Report: PMB-26-909

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Reference	PMB-26-909
Title	Avenacosidase from oat: purification, sequence analysis and biochemical characterization of a new member of the BGA family of beta-glucosidases
Journal	Plant Molecular Biology
Year	1994
Volume	26
Pages	909-921
Author	Gus-Mayer S Brunner H Schneider-Poetsch H Rudiger W
Abstract	A protein consisting of 60 kDa subunits (As-P60) was isolated from etiolated oat seedlings (Avena sativa L. and characterized as avenacosidase, a beta-glucosidase that belongs to a preformed defence system of oat against fungal infection The enzyme is highly aggregated; it consists of 300-350 kDa aggregates and multimers thereof Dissociation by freezing/thawing leads to complete loss of enzyme activity The specificity of the enzyme was investigated with para-nitrophenyl derivatives which serve as substrates, in decreasing order beta-fucoside, beta-glucoside, beta-galactoside, beta-xyloside The corresponding orthonitrophenyl glycosides are less well accepted No hydrolysis was found with a-glycosides and beta-thioglucoside An anti-As-P60 antiserum was prepared and used for isolation of a cDNA clone coding for As-P60. A presequence of 55 amino acid residues was deduced from comparison of the cDNA sequence with the N-terminal sequence determined by Edman degradation of the mature protein. The presequence has the characteristics of a stroma-directing signal peptide; localization of As-P60 in plastids of oat seedlings was confirmed by western blotting. The amino acid sequence revealed significant homology (> 39% sequence identity) to beta-glucosidases that are constituents of a defence mechanism in dicotyledonous plants. 34% sequence identity was even found with mammalian and bacterial beta-glucosidases of the BGA family. Avenacosidase extends the occurrence of this family of beta-glucosidases to monocotyledonous plants.
Keyword	amino acid sequence [ Show all 9 ]

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