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. 1986 Apr;83(7):2081–2085. doi: 10.1073/pnas.83.7.2081

Primary structure of the (1→3,1→4)-β-D-glucan 4-glucohydrolase from barley aleurone

Geoffrey B Fincher *, Peter A Lock *, Margaret M Morgan *, Klaus Lingelbach *, Richard E H Wettenhall *, Julian F B Mercer †, Anders Brandt ‡, Karl Kristian Thomsen ‡
PMCID: PMC323234  PMID: 16593676

Abstract

During germination of barley grains, the cell walls of the starchy endosperm are degraded by (1→3,1→4)-β-glucanases (EC 3.2.1.73) secreted from the aleurone and scutellar tissues. The complete sequence of the aleurone (1→3,1→4)-β-glucanase isoenzyme II comprises 306 amino acids and was determined by sequencing nine tryptic peptides (110 residues) and aligning them with the amino acid sequence deduced from a cDNA clone encoding the 291 NH2-terminal residues. Although no amino acid sequence homology with a bacterial (1→3)(1→4)-β-glucanase is apparent, close to 50% homology is found with two large regions of a (1→3)-β-glucanase from tobacco pith tissue. The gene for barley (1→3,1→4)-β-glucanase isoenzyme II shares with that for the α-amylase isoenzyme 1 a strongly preferred use of codons with G and C in the wobble position (94% and 90%, respectively). Both enzymes are secreted from the aleurone cells during germination. Such one-sided codon usage is not characteristic for the gene encoding the (1→3)-β-glucanase of tobacco pith tissue or the hor2-4 gene encoding the B1 hordein storage protein in the endosperm.

Keywords: cell-wall degradation, cDNA, codon usage, tissue specificity

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Selected References

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