Abstract
Two cDNAs have been isolated from libraries generated from poly(A) +RNA of young barley roots and leaves, using a cDNA encoding barley (1 → 3)-β-glucanase isoenzyme GII as a probe. Nucleotide sequence analyses and ribonuclease protection assays show that the two cDNAs differ only in the length of their 3′-untranslated regions; the corresponding mRNAs are likely to originate from a single gene by tissue-specific processing at separate polyadenylation sites. When the coding region of the cDNA is expressed in E. coli, the resultant protein catalyses the hydrolysis of (1 → 3)-β-glucan with an action pattern characteristic of a (1 → 3)-β-glucan endohydrolase (EC 3.2.1.39). The enzyme has been designated isoenzyme GV of the barley (1 → 3)-β-glucanase family.
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