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Structural basis of the antifungal activity of wheat PR4 proteins
Author(s) -
Bertini Laura,
Caporale Carlo,
Testa Marco,
Proietti Silvia,
Caruso Carla
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.07.045
Subject(s) - ribonuclease , fusarium culmorum , docking (animal) , antifungal , biochemistry , in vitro , fusarium , fungal pathogen , spore , active site , chemistry , pathogen , microbiology and biotechnology , biology , enzyme , rna , botany , gene , medicine , nursing
PR4 proteins possess antifungal activity against several pathogenic fungi suggesting a pivotal role in defence reactions against plant pathogen attack. We already showed that wheatwin1, a wheat PR protein of class 4, is endowed with ribonuclease activity. In this study we produced three mutants altering the active site and performed comparative analysis with the native protein also in the presence of the ribonuclease inhibitor 5′‐ADP. We characterized the RNA binding site and its interaction with 5′‐ADP by 3D modelling and docking studies. Moreover, in vitro antifungal assays have been carried out in order to study the relationship between antifungal and ribonuclease activities. Finally, localization of wheatwin1 in Fusarium culmorum spores was evaluated using fluorescence light microscope.