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oai:docta.ucm.es:20.500.14352/137332023-08-11T05:03:02Zcom_20.500.14352_14col_20.500.14352_15

00925njm 22002777a 4500 dc Ruggiero, Alessia author García-Ortega, Lucía author Moreira, Miguel author Ragucci, Sara author Landi, Nicola author Di Marco, Antimo author Berisio, Rita author 2019-09-01 Ribotoxins are fungal proteins that serve as weapons against parasites and insects. They are strongly toxic due to their ability to enter host cells and inactivate ribosomes. Ageritin is the prototype of a new ribotoxin-like protein family present in basidiomycetes. We demonstrate that this enzyme has peculiar binding and enzymatic features. Different from other ribotoxins, its ribonucleolytic activity requires the presence of divalent cations, with a maximum activation in the presence of zinc ions, for which Ageritin exhibits the strongest affinity of binding. We modeled the catalytic metal binding site of Ageritin, made of the putative triad Asp68, Asp70 and His77. This report highlights that Ageritin has the structure and function of an RNase but a Mg2+/Zn2+-dependent mechanism of action, a new finding for ribotoxins. As a zinc-dependent toxin, Ageritin can be classified among the arsenal of zinc-binding proteins involved in fungal virulence. 0141-8130, ESSN: 1879-0003 10.1016/j.ijbiomac.2019.06.125 https://hdl.handle.net/20.500.14352/13733 https://www.sciencedirect.com/science/article/pii/S0141813019324468 Binding and enzymatic properties of Ageritin, a fungal ribotoxin with novel zinc-dependent function