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Evrard, A.; Lagarde, V.; Joudrier, P.; Gautier, M.F.. |
Puroindolines are two small, basic cysteine-rich proteins isolated from Triticum aestivum seeds and characterized by a tryptophan-rich domain. They form the molecular basis of wheat grain hardness and display antimicrobial activity that may contribute to plant defence. Their antimicrobial activity is presumed to be due to their hydrophobic tryptophan-rich domain. However, little is known about their mode of action and there is no in vivo evidence that the binding of puroindolines to membranes is mediated by their tryptophan-rich domain. In this study, using a yeast complementation assay, we showed that puroindolines interact with the Saccharomyces cerevisiae plasma membrane. By site-directed mutagenesis of their tryptophan-rich domain, we determined that... |
Tipo: Journal Article |
Palavras-chave: SACCHAROMYCES CEREVISIAE. |
Ano: 2008 |
URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD20093e8d01c9&uri=/notices/prodinra1/2009/03/ |
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