RT Journal Article
T1 Binding and enzymatic properties of Ageritin, a fungal ribotoxin with novel zinc-dependent function
A1 Ruggiero, Alessia
A1 García-Ortega, Lucía
A1 Moreira, Miguel
A1 Ragucci, Sara
A1 Landi, Nicola
A1 Di Marco, Antimo
A1 Berisio, Rita
AB 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.
PB Elsevier
SN 0141-8130, ESSN: 1879-0003
YR 2019
FD 2019-09-01
LK https://hdl.handle.net/20.500.14352/13733
UL https://hdl.handle.net/20.500.14352/13733
LA eng
NO Universidad Complutense de Madrid / Banco de Santander
NO Università degli Studi de la Campania Luigi  Vanvitelli (Caserta, Italia)
DS Docta Complutense
RD 8 abr 2025