RT Journal Article
T1 Structural and enzymatic properties of Ageritin, a novel metal-dependent ribotoxin-like protein with antitumor activity
A1 Ruggiero, Alessia
A1 García Ortega, Lucía
A1 Ragucci, Sara
A1 Russo, Rosita
A1 Landi, Nicola
A1 Berisio, Rita
A1 Di Maro, Antimo
AB Ageritin has been recently described as the first ribotoxin-like from Basidiomycota division (mushroom Agrocybe aegerita) with known antitumor activity (BBA 2017, 1861: 1113-1121). By investigating structural, catalytic and binding properties, we demonstrate that Ageritin is a unique ribotoxin-like protein. Indeed, typical of the ribotoxin family, it shows the specific ribonucleolytic activity against the ribosomal Sarcin-Ricin Loop in a rabbit reticulocytes assay. However, it displays several elements of novelty, as this activity is strongly metal-dependent and completely suppressed in the presence of EDTA, different from other representative members of the ribotoxin family. Consistently, we prove that Ageritin is able to bind magnesium ions with low micromolar affinity. We also show that Ageritin is significantly more stable than other ribotoxins in thermal and chemical denaturation experiments. These peculiar features make Ageritin the prototype of a new ribotoxin-like family present in basidiomycetes. Finally, given its high stability, this enzyme is a promising candidate as a new tool in immunoconjugates and nanoconstructs.
PB Elsevier
YR 2018
FD 2018-09-18
LK https://hdl.handle.net/20.500.14352/131305
UL https://hdl.handle.net/20.500.14352/131305
LA eng
NO Alessia Ruggiero, Lucía García-Ortega, Sara Ragucci, Rosita Russo, Nicola Landi, Rita Berisio, Antimo Di Maro, Structural and enzymatic properties of Ageritin, a novel metal-dependent ribotoxin-like protein with antitumor activity, Biochimica et Biophysica Acta (BBA) - General Subjects, Volume 1862, Issue 12, 2018, Pages 2888-2894
NO Santander- Universidad Complutense de Madrid
DS Docta Complutense
RD 17 mar 2026