We have cloned and sequenced a full-length cDNA from barley (Hordeum vulgate L.) seeds encoding the bifunctional ~-amylase/subtilisin inhibitor (BASI). The nucleotide sequence predicts an open reading frame coding for a protein of 203 amino acids. The first 22 amino acids exhibit the sequence charac
Nucleotide sequence of a cDNA coding for the barley seed protein CMa: an inhibitor of insect α-amylase
✍ Scribed by Søren K. Rasmussen; Anette Johansson
- Publisher
- Springer
- Year
- 1992
- Tongue
- English
- Weight
- 361 KB
- Volume
- 18
- Category
- Article
- ISSN
- 0167-4412
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✦ Synopsis
The primary structure of the insect alpha-amylase inhibitor CMa of barley seeds was deduced from a full-length cDNA clone pc43F6. Analysis of RNA from barley endosperm shows high levels 15 and 20 days after flowering. The cDNA predicts an amino acid sequence of 119 residues preceded by a signal peptide of 25 amino acids. Ala and Leu account for 55% of the signal peptide. CMa is 60-85% identical with alpha-amylase inhibitors of wheat, but shows less than 50% identity to trypsin inhibitors of barley and wheat. The 10 Cys residues are located in identical positions compared to the cereal inhibitor family with a Pro-X-Cys motif present in all.
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