RT info:eu-repo/semantics/article T1 The biological action and structural characterization of eryngitin 3 and 4, ribotoxin-like proteins from Pleurotus eryngii fruiting bodies A1 Ragucci, Sara A1 Landi, Nicola A1 Citores González, Lucía A1 Iglesias Álvarez, María del Rosario A1 Russo, Rosita A1 Clemente, Angela A1 Saviano, Michele A1 Pedone, Paolo Vincenzo A1 Chambery, Angela A1 Ferreras Rodríguez, José Miguel A1 Di Maro, Antimo K1 Amino acid sequence K1 Molds (Fungi) K1 Mushrooms K1 Setas K1 Mass spectrometry K1 Espectrometría de masas K1 Ribotoxin K1 Proteins K1 2302.02 Aminoácidos K1 2414.09 Mohos K1 2414.06 Hongos K1 2302.27 Proteínas K1 2415 Biología Molecular AB Ribotoxin-like proteins (RL-Ps) are specific ribonucleases found in mushrooms that are able to cleave a single phosphodiester bond located in the sarcin–ricin loop (SRL) of the large rRNA. The cleaved SRL interacts differently with some ribosomal proteins (P-stalk). This action blocks protein synthesis because the damaged ribosomes are unable to interact with elongation factors. Here, the amino acid sequences of eryngitin 3 and 4, RL-Ps isolated from Pleurotus eryngii fruiting bodies, were determined to (i) obtain structural information on this specific ribonuclease family from edible mushrooms and (ii) explore the structural determinants which justify their different biological and antipathogenic activities. Indeed, eryngitin 3 exhibited higher toxicity with respect to eryngitin 4 against tumoral cell lines and model fungi. Structurally, eryngitin 3 and 4 consist of 132 amino acids, most of them identical and exhibiting a single free cysteinyl residue. The amino acidic differences between the two toxins are (i) an additional phenylalanyl residue at the N-terminus of eryngitin 3, not retrieved in eryngitin 4, and (ii) an additional arginyl residue at the C-terminus of eryngitin 4, not retrieved in eryngitin 3. The 3D models of eryngitins show slight differences at the N- and C-terminal regions. In particular, the positive electrostatic surface at the C-terminal of eryngitin 4 is due to the additional arginyl residue not retrieved in eryngitin 3. This additional positive charge could interfere with the binding to the SRL (substrate) or with some ribosomal proteins (P-stalk structure) during substrate recognition. PB MDPI SN 1422-0067 YR 2023 FD 2023 LK https://uvadoc.uva.es/handle/10324/66860 UL https://uvadoc.uva.es/handle/10324/66860 LA eng NO International Journal of Molecular Sciences, 2023, Vol. 24, Nº. 19, 14435 NO Producción Científica DS UVaDOC RD 06-oct-2024