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GrainGenes Reference Report: PLT-169-51

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Reference
PLT-169-51
Title
Selective expression of a probable Amylase-protease inhibitor in barley Hordeum-vulgare aleurone cells comparison to the barley Amylase-subtilisin inhibitor
Journal
Planta
Year
1986
Volume
169
Pages
51-63
Author
Mundy J
Rogers JC
Abstract
We have cloned and sequenced a 650-nucleotide cDNA from barley (Hordeum vulgare L.) aleurone layers encoding a protein that is closely related to a known .alpha.-amylase inhibitor from Indian finger millet (Eleusine coracana Gaertn.), and that has homologies to certain plant trypsin inhibitors. mRNA for this probable amylase/protease inhibitor (PAPI) is expressed primarily in aleurone tissue during late development of the grain, as compared to that for the amylase/subtilisin inhibitor, which is expressed in endosperm during the peak of storage-protein synthesis. PAPI mRNA is present at high levels in aleurone tissue of dessicated, mature grain, and in incubated aleurone layers prepared from rehydrated mature seeds. Its expression in those layers is not affected by either abscisic acid or gibberellic acid, hormones that, respectively, increase and decrease the abundance of mRNA for the amylase/subtilisin inhibitor. PAPI mRNA is also as abundant in gibberellic acid-treated aleurone layers as that for .alpha.-amylase, and PAPI protein is synthesized in that tissue at levels that are comparable to .alpha.-amylase. PAPI protein is secreted from aleurone layers into the incubation medium.
Probe
A1f
Alf
Keyword
Abscisic-acid
Complementary DNA
Eleusine-coracana
Gibberellic-acid
Subtilisin

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