Binding and enzymatic properties of Ageritin, a fungal ribotoxin with novel zinc-dependent function



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Ruggiero, Alessia and García-Ortega, Lucía and Moreira, Miguel and Ragucci, Sara and Landi, Nicola and Di Marco, Antimo and Berisio, Rita (2019) Binding and enzymatic properties of Ageritin, a fungal ribotoxin with novel zinc-dependent function. International Journal of Biological Macromolecules, 136 . pp. 625-631. ISSN 0141-8130, ESSN: 1879-0003

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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.

Item Type:Article
Uncontrolled Keywords:Metal-binding protein; Ribotoxins; Ribonuclease activity
Subjects:Medical sciences > Biology > Molecular biology
Medical sciences > Biology > Biochemistry
ID Code:57527
Deposited On:30 Oct 2019 13:12
Last Modified:30 Oct 2019 13:12

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