Publications by authors named "Erosantonio Lampitella"
Conformational stability of ageritin, a metal binding ribotoxin-like protein of fungal origin.
Int J Biol Macromol
November 2022
Article Synopsis
- Ageritin is a protein from edible mushrooms that functions as a ribotoxin and requires zinc ions for its enzymatic activity, which involves breaking specific bonds in ribosomes.
- Research on ageritin's stability across different pH levels showed it has high thermal stability with a denaturation temperature of 78°C and a Gibbs energy value of 36 kJ/mol at pH 5.0.
- The study also looked at a modified form of ageritin where a specific cysteine was altered; although this form maintained enzymatic activity, it demonstrated lower stability and highlighted the significance of zinc in maintaining the protein's structure.
Ageritin is the prototype of a new ribotoxin-like protein family, which has been recently identified also in basidiomycetes. The protein exhibits specific RNase activity through the cleavage of a single phosphodiester bond located at sarcin/ricin loop of the large rRNA, thus inhibiting protein biosynthesis at early stages. Conversely to other ribotoxins, its activity requires the presence of divalent cations.
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