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Title
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Biochemical and molecular characterization of three barley seed proteins with antifungal properties.
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Authors
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R.Leah,
H.Tommerup,
I.Svendsen,
J.Mundy.
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Ref.
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J Biol Chem, 1991,
266,
1564-1573.
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PubMed id
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Abstract
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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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