Binding and enzymatic properties of Ageritin, a fungal ribotoxin with novel zinc-dependent function
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Binding and enzymatic properties of Ageritin, a fungal ribotoxin with novel zinc-dependent function (430 views)

Ruggiero A, Garcia-ortega L, Moreira M, Ragucci S, Landi N, Di Maro A, Berisio R

Int J Biol Macromol (ISSN: 0141-8130linking, 1879-0003electronic), 2019 Jun 18; 136: 625-631.

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Paper type: Journal Article,

Impact factor: 4.78, 5-year impact factor: 4.73

Url: Not available.

Keywords: Metal-Binding Protein, Ribonuclease Activity, Ribotoxins,

Affiliations:
*** IBB - CNR ***

Istituto di Biostrutture e Bioimmagini, C.N.R., Via Mezzocannone 16, I-80134 Napoli, 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., Department of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania 'Luigi Vanvitelli', Via Vivaldi 43, I-81100 Caserta, Italy. Electronic address: rita.berisio@cnr.it., Istituto di Biostrutture e Bioimmagini, C.N.R., Via Mezzocannone 16, I-80134 Napoli, Italy. Electronic address: antimo.dimaro@unicampania.it.,


References:
Not available.
Binding and enzymatic properties of Ageritin, a fungal ribotoxin with novel zinc-dependent function

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 Mg(2+)/Zn(2+)-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.
Binding and enzymatic properties of Ageritin, a fungal ribotoxin with novel zinc-dependent function

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

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Ruggiero A, Garcia-ortega L, Ragucci S, Russo R, Landi N, Berisio R, Di Maro A
* Structural and enzymatic properties of Ageritin, a novel metal-dependent ribotoxin-like protein with antitumor activity (474 views)
Bba-Gen Subjects (ISSN: 1872-8006electronic, 0304-4165linking, 0304-4165print), 2018 Sep 18; 1862(12): 2888-2894.
Impact Factor: 3.679
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Pastore C, Franzese M, Sica F, Temussi P, Pastore A
* Understanding the binding properties of an unusual metal-binding protein - a study of bacterial frataxin (705 views)
Febs Journal (ISSN: 1742-464x), 2007 Sep; 274(16): 4199-4210.
Impact Factor: 3.396
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2 Records (2 excluding Abstracts).
Total impact factor: 7.075 (7.075 excluding Abstracts).
Total 5 year impact factor: 8.215 (8.215 excluding Abstracts).

Last modified by Rita Berisio on Sunday 12 July 2020, 13:14:40
430 views. Last view on Sunday 01 December 2024, 4:57:20