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Analysis of two novel classes of plant antifungal proteins from radish (Raphanus sativus L.) seeds.

Franky R. G. TerrasF.A. Janssens Laboratory of Genetics, Catholic University of Leuven, Heverlee BelgiumH. SchoofsF.A. Janssens Laboratory of Genetics, Catholic University of Leuven, Heverlee BelgiumM F De BolleF.A. Janssens Laboratory of Genetics, Catholic University of Leuven, Heverlee BelgiumF. Van LeuvenF.A. Janssens Laboratory of Genetics, Catholic University of Leuven, Heverlee BelgiumSarah B. ReesF.A. Janssens Laboratory of Genetics, Catholic University of Leuven, Heverlee BelgiumJozef VanderleydenF.A. Janssens Laboratory of Genetics, Catholic University of Leuven, Heverlee BelgiumBruno P.A. CammueF.A. Janssens Laboratory of Genetics, Catholic University of Leuven, Heverlee BelgiumW. F. BroekaertF.A. Janssens Laboratory of Genetics, Catholic University of Leuven, Heverlee Belgium
1992en
ABI

Аннотация

Two novel classes of antifungal proteins were isolated from radish seeds. The first class consists of two homologous proteins (Rs-AFP1 and Rs-AFP2) that were purified to homogeneity. They are highly basic oligomeric proteins composed of small (5-kDa) polypeptides that are rich in cysteine. Both Rs-AFPs have a broad antifungal spectrum and are among the most potent antifungal proteins hitherto characterized. In comparison with many other plant antifungal proteins, the activity of the Rs-AFPs is less sensitive to the presence of cations. Moreover, their antibiotic activity shows a high degree of specificity to filamentous fungi. The amino-terminal regions of the Rs-AFPs show homology with the derived amino acid sequences of two pea genes specifically induced upon fungal attack, to gamma-thionins and to sorghum alpha-amylase inhibitors. The radish 2S storage albumins were identified as the second novel class of antifungal proteins. All isoforms inhibit growth of different plant pathogenic fungi and some bacteria. However, their antimicrobial activities are strongly antagonized by cations.

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