The fuc1 gene product (20kDa FUC1) of Pisum sativum has no α-L-fucosidase activity

The fuc1 gene product (20kDa FUC1) of Pisum sativum has no α-L-fucosidase activity An α-L-fucosidase purified from pea (Pisum sativum L. cv Alaska) epicotyl was previously described as a cell wall enzyme of 20 kDa that hydrolyses terminal α-L-fucosidic linkages from oligosaccharide fragments of xyloglucan. cDNA and genomic copies were further isolated and sequenced. The predicted product of the cDNA and the genomic clone (fuc1), was a 20 kDa protein containing a signal peptide and five cysteines. This was the first α-L-fucosidase gene to be cloned in plants but its fucosidase activity has not been demonstrated. Here, our biochemical and immuno analyses suggest that fuc1 does not encode an α-L-fucosidase. Pea fuc1 expressed in Escherichia coli, insect cells and Arabidopsis thaliana produced recombinant proteins without α-L-fucosidase activity. Pea plants had endogenous α-L-fucosidase activity, but the enzyme was not recognised by an antibody produced against recombinant FUC1 protein expressed in E. coli. In contrast, the antibody immunoprecipitated a 20 kDa protein which was inactive. By chromatographic analysis of pea protein extracts, we separated α-L-fucosidase-active fractions from the 20 kDa protein fractions. We conclude that the α-L-fucosidase activity is not attributable to the 20 kDa FUC1 protein. A new function for fuc1 gene product, now named PIP20 (for protease inhibitor from pea) is proposed. Plant Molecular Biology Springer Journals

The fuc1 gene product (20kDa FUC1) of Pisum sativum has no α-L-fucosidase activity

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Kluwer Academic Publishers
Copyright © 2003 by Kluwer Academic Publishers
Life Sciences; Biochemistry, general; Plant Sciences; Plant Pathology
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