Expression of functional Raphanus sativus antifungal protein in yeast

FEBS Letters

Vilas Alves, Ana L.¹  De Samblanx, Genoveva W.¹  Broekaert, Willem F.¹  Cammue, Bruno P.A.¹  Terras, Franky R.G.¹ 

[1] F.A. Janssens Laboratory of Genetics, Catholic University of Leuven, Willem de Croylaan 42, B-3001 Heverlee, Belgium

关键词: Mutagenesis;    Polymerase chain reaction;    Saccharomyces cerevisiae;    Mating factor;    Rs-AFP;    Raphanus sativus antifungal protein;    IC50;    protein concentration required for 50% inhibition of fungal growth;   

DOI  :  10.1016/0014-5793(94)00597-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Rs-AFP2 is a 51 amino acid cysteine-rich peptide isolated from radish (Raphanus sativus) seeds that exhibits potent inhibitory activity against filamentous fungi. A cDNA clone encoding the Rs-AFP2 preprotein was modified by recombinant DNA methods to allow expression in the yeast Saccharomyces cerevisiae. This peptide was expressed in yeast as a fusion protein carrying at its N-terminus the prepro-sequences derived from the precursor of the yeast pheromone mating factor α1. These sequences allow secretion of the biologically active peptide in a correctly processed form. Deletion of the mating factor α1 pro-peptide drastically reduced the expression level of the peptide.

【 授权许可】

Unknown