In:
Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 83, No. 7 ( 1986-04), p. 2081-2085
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 NH 2 -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 B 1 hordein storage protein in the endosperm.
Type of Medium:
Online Resource
ISSN:
0027-8424
,
1091-6490
DOI:
10.1073/pnas.83.7.2081
Language:
English
Publisher:
Proceedings of the National Academy of Sciences
Publication Date:
1986
detail.hit.zdb_id:
209104-5
detail.hit.zdb_id:
1461794-8
SSG:
11
SSG:
12
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