2026-04-26T22:01:45Zhttps://uvadoc.uva.es/oai/request

oai:uvadoc.uva.es:10324/668602024-03-20T20:00:34Zcom_10324_1134com_10324_931com_10324_894col_10324_1213

Ragucci, Sara Landi, Nicola Citores González, Lucía Iglesias Álvarez, María del Rosario Russo, Rosita Clemente, Angela Saviano, Michele Pedone, Paolo Vincenzo Chambery, Angela Ferreras Rodríguez, José Miguel Di Maro, Antimo 2024-03-20T12:29:54Z 2024-03-20T12:29:54Z 2023 International Journal of Molecular Sciences, 2023, Vol. 24, Nº. 19, 14435 1422-0067 https://uvadoc.uva.es/handle/10324/66860 10.3390/ijms241914435 14435 19 International Journal of Molecular Sciences 24 1422-0067 Producción Científica 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. Unión Europea NextGenerationEU - (Project IR0000009) Ministero dell’Università e della Ricerca (MUR), Prin 2022 PNRR - (project P2022YERKR) Junta de Castilla y León, Consejería de Educación - (Grant VA033G19) application/pdf eng MDPI info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/4.0/ © 2023 The authors Atribución 4.0 Internacional Amino acid sequence Molds (Fungi) Mushrooms Setas Mass spectrometry Espectrometría de masas Ribotoxin Proteins 2302.02 Aminoácidos 2414.09 Mohos 2414.06 Hongos 2302.27 Proteínas 2415 Biología Molecular The biological action and structural characterization of eryngitin 3 and 4, ribotoxin-like proteins from Pleurotus eryngii fruiting bodies info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion https://www.mdpi.com/1422-0067/24/19/14435 SI