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GrainGenes Reference Report: PMB-12-673

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Reference	PMB-12-673
Title	The bifunctional alpha amylase-subtilisin inhibitor of barley nucleotide sequence and patterns of seed-specific expression
Journal	Plant Molecular Biology
Year	1989
Volume	12
Pages	673-682
Author	Leah R Mundy J
Type	Article
Language	English
Abstract	We have cloned and sequenced a full-length cDNA from barley (Hordeum vulgare L.) seeds encoding the bifunctional .alpha.- 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 characteristic of a signal peptide, as found in several other plant protease inhibitors. Northern blot hybridization experiments indicate that BASI mRNA accumulation is strictly tissue-specific and is developmentally programmed. BASI mRNA transcripts were only identified in 1) developing starchy endosperm tissue from 14 days after flowering and 2) aleurone tissue of germinating seeds. In this latter tissue, BASI mRNA accumulation is enhanced by abscisic acid and abolished by gibberellic acid. Expression of BASI mRNA was also studied in the lys 3a high-lysine barley mutants Riso No. 1508 and Piggy. These high-lysine barleys show 2-4-fold higher levels as well as prolonged accumulation of BASI mRNA compared to the normal motherline Bomi. This correlates with the increased deposition of BASI protein in lys 3a barley mutants. Genomic blot analysis of barley DNA suggests that there are one or two BASI structural genes per haploid genome. Possible roles of BASI as part of a defence mechanism against precocious germination and pathogens are discussed.
Probe	BASI cDNA pcCHI26
Keyword	Genetics Hordeum-vulgare Molecular sequence data

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