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Biochemical and molecular characterization of three barley seed proteins with antifungal properties
We have purified three proteins from barley (Hordeum vulgare L.) seeds which synergistically inhibit the growth of fungi measured in a microtiter well assay. The proteins are a 26-kDa chitinase, a 30-kDa ribosome-inactivating protein, and a 32-kDa (1-3)-beta-glucanase. Full-length cDNAs encoding the...
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Published in: | The Journal of biological chemistry 1991-01, Vol.266 (3), p.1564-1573 |
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Main Authors: | , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | We have purified three proteins from barley (Hordeum vulgare L.) seeds which synergistically inhibit the growth of fungi measured
in a microtiter well assay. The proteins are a 26-kDa chitinase, a 30-kDa ribosome-inactivating protein, and a 32-kDa (1-3)-beta-glucanase.
Full-length cDNAs encoding them were isolated and sequenced to determine the complete primary structures of the proteins.
Northern hybridizations with the cDNAs as probes showed that the corresponding mRNAs accumulate differentially during seed
development and germination. Chitinase mRNA accumulates to high levels in aleurone cells during late seed development and
early germination, while high levels of mRNA encoding the ribosome-inactivating protein accumulate only in the starchy endosperm
during late seed development. The glucanase mRNA accumulates to low levels during seed development and to higher levels in
aleurone and seedling tissues during germination. Southern hybridizations showed that the three proteins are encoded by small
families of three to eight genes. Their biological roles and potential use in genetic engineering studies are discussed. |
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ISSN: | 0021-9258 1083-351X |
DOI: | 10.1016/S0021-9258(18)52331-0 |