Structural and enzymatic properties of Ageritin, a novel metal-dependent ribotoxin-like protein with antitumor activity(147 visite) Ruggiero A, Garcia-ortega L, Ragucci S, Russo R, Landi N, Berisio R, Di Maro A
Tipo di articolo: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 3.679, Impact factor a 5 anni: 4.81
Url: Non disponibile.
Parole chiave: Ageritin, Agrocybe Aegerita, Metal-Protein, Protein Stability, Ribonuclease Activity, Ribotoxins, Agrocybe Chemistry
, Antineoplastic Agents Chemistry Pharmacology
, Circular Dichroism
, Electrophoresis, Polyacrylamide Gel
, Magnesium Metabolism
, Protein Binding
, Protein Structure, Secondary
, Ribonucleases Chemistry Pharmacology
, Ribosomes Drug Effects Metabolism
, Spectrophotometry, Ultraviolet
, Biological Chemistry Pharmacology,
*** IBB - CNR *** Institute of Biostructures and Bioimaging, National Research Council, Via Mezzocannone, 16, I-80134 Naples, Italy., Departamento de Bioquimica y Biologia Molecular, Facultad de Quimica, Universidad Complutense, E-28040 Madrid, Spain., Department of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania 'Luigi Vanvitelli', Via Vivaldi 43, I-81100 Caserta, Italy., Institute of Biostructures and Bioimaging, National Research Council, Via Mezzocannone, 16, I-80134 Naples, Italy. Electronic address: firstname.lastname@example.org., Department of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania 'Luigi Vanvitelli', Via Vivaldi 43, I-81100 Caserta, Italy. Electronic address: email@example.com.,
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.
Aloj L, Aurilio M, Rinaldi V, D'Ambrosio L, Tesauro D, Peitl PK, Maina T, Mansi R, Von Guggenberg E, Joosten L, Sosabowski JK, Breeman WA, De Blois E, Koelewijn S, Melis M, Waser B, Beetschen K, Reubi JC, De Jong M * The EEE project(330 visite) Proc Int Cosm Ray Conf Icrc Universidad Nacional Autonoma De Mexico, 2007; 5(HEPART2): 977-980. Impact Factor:0 DettagliEsporta in BibTeXEsporta in EndNote
98 Records (96 escludendo Abstract e Conferenze). Impact factor totale: 367.408 (361.21 escludendo Abstract e Conferenze). Impact factor a 5 anni totale: 375.366 (368.292 escludendo Abstract e Conferenze).