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GrainGenes Reference Report: PLC-2-769

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Reference	PLC-2-769
Title	Hormonal regulation processing and secretion of cysteine proteinases in barley aleurone layers
Journal	Plant Cell
Year	1990
Volume	2
Pages	769-784
Author	Koehler SM Ho THD
Type	Article
Language	English
Abstract	Barley aleurone layers synthesize and secrete several proteases in response to gibberellic acid (GA3). Two major cysteine proteinases designated EP-A (37,000 Mr) and EP-B (30,000 Mr) have been described [Koehler and Ho (1988). Plant Physiol. 87, 95-103]. We now report the cDNA cloning of EP-B and describe the post-translational processing and hormonal regulation of both cysteine proteinases. Three cDNAs for cysteine proteinases were cloned from GA3-induced barley aleurone layers. Genomic DNA gel blot analysis indicated that these are members of a small gene family with no more than four to five different genes. The proteins encoded by two of these clones, pHVEP1 and 4, are 98% similar to each other and are isozymes of EP-B. The proteins contain large preprosequences followed by the amino acid sequence described as the mature N terminus of purified EP-B, and are antigenic to EP-B antiserum. The results of pulse- chase experiments indicated that the post-translational processing of large prosequences proceeds in a multistep fashion to produce the mature enzymes. Processing intermediates for EP-B are observed both in the aleurone layers and surrounding incubation medium, but only mature EP-A is secreted. The regulation of synthesis of EP-A, EP-B, and other aleurone cysteine proteinases was compared at the protein and mRNA levels. We conclude that barley aleurone cysteine proteinase are differentially regulated with respect to their temporal and hormonally induced expression.
Probe	pHVEP1 pHVEP4 pHVEP7
Keyword	Blot analysis [ Show all 6 ]

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