Binder Ulrike, Benčina Mojca, Fizil Ádám, Batta Gyula, Chhillar Anil K, Marx Florentine
Biocenter, Division of Molecular Biology, Medical University of Innsbruck, Innrain 80, A-6020 Innsbruck, Austria; Division of Hygiene and Medical Microbiology, Schöpfstrasse 41, Medical University of Innsbruck, A-6020 Innsbruck, Austria.
Department of Biotechnology, National Institute of Chemistry, Hajdrihova 19, SI-1000 Ljubljana, Slovenia.
FEBS Lett. 2015 May 8;589(11):1266-71. doi: 10.1016/j.febslet.2015.03.037. Epub 2015 Apr 14.
The Penicillium chrysogenum antifungal protein PAF is toxic against potentially pathogenic Ascomycetes. We used the highly sensitive aequorin-expressing model Aspergillus niger to identify a defined change in cytoplasmic free Ca(2+) dynamics in response to PAF. This Ca(2+) signature depended on an intact positively charged lysine-rich PAF motif. By combining Ca(2+) measurements in A. niger mutants with deregulated cAMP/protein kinase A (PKA) signaling, we proved the interconnection of Ca(2+) perturbation and cAMP/PKA signaling in the mechanistic function of PAF. A deep understanding of the mode of action of PAF is an invaluable prerequisite for its future application as new antifungal drug.