Volume 30, Number 2, 229-241, DOI: 10.1007/BF00020110

Molecular cloning and characterization of a gibberellin-inducible, putative α-glucosidase gene from barley

Brian K. Tibbot and Ronald W. Skadsen

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Abstract

A putative agr-glucosidase clone has been isolated from a cDNA library constructed from mRNA of barley aleurones treated with gibberellin A3 (GA). The clone is 2752 bp in length and has an uninterrupted open reading frame encoding a polypeptide of 877 amino acids. A 680 amino acid region is 43% identical to human lysosomal agr-glucosidase and other glycosyl hydrolases. In isolated aleurones, the levels of the corresponding mRNA increase strongly after the application of GA, similar to the pattern exhibited by low-pI agr-amylase mRNA. High levels are also observed in the aleurone and scutellum after germination, while low levels are found in developing seeds. The genome contains a single form of this agr-glucosidase gene and two additional sequences that may be related genes or pseudogenes.

Key words  agr-amylase - barley - GA - gene-expression - agr-glucosidase - maltase

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