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A tobacco mosaic virus-induced tobacco protein is homologous to the sweet-tasting protein thaumatin

Naturevolume 321pages531532 (1986) | Download Citation



Infection of tobacco plants with tobacco mosaic virus (TMV) results in an increase in the activities of several enzymes and induces the de novo synthesis of about 10 proteins that are protease-resistant and soluble at pH3. These proteins accumulate in the intercellular leaf space1,2. The appearance of pathogenesis-related (PR) proteins is closely associated with the phenomenon of ‘systemic acquired resistance’ and it has been suggested that such proteins have an antiviral function3,4. Previously, we cloned complementary DNAs to the messenger RNAs for the three smallest PR proteins, PR-1a, -1b and -1c, and these clones were used to show that there is an increase of more than 100-fold in the concentration of PR-1 mRNAs following TMV infection of tobacco5,6. Here, we describe the cDNA cloning of another mRNA whose synthesis is induced by TMV infection. Sequencing of the cDNA showed that the encoded protein is highly homologous to thaumatin, the intensely sweet-tasting protein from the fruits of the monocot Thaumatococcus daniellii Benth, a West African rainforest shrub. The conservation of a gene encoding a thaumatin-like protein in tobacco suggests that the encoded protein may have a more general function than that of being sweet-tasting.

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  1. Department of Biochemistry, State University of Leiden, PO Box 9505, Leiden, The Netherlands

    • Ben J. C. Cornelissen
    • , Rob A. M. Hooft van Huijsduijnen
    •  & John F. Bol


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