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Título
The biological action and structural characterization of eryngitin 3 and 4, ribotoxin-like proteins from Pleurotus eryngii fruiting bodies
Autor
Año del Documento
2023
Editorial
MDPI
Descripción
Producción Científica
Documento Fuente
International Journal of Molecular Sciences, 2023, Vol. 24, Nº. 19, 14435
Abstract
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.
Materias (normalizadas)
Amino acid sequence
Molds (Fungi)
Mushrooms
Setas
Mass spectrometry
Espectrometría de masas
Ribotoxin
Proteins
Materias Unesco
2302.02 Aminoácidos
2414.09 Mohos
2414.06 Hongos
2302.27 Proteínas
2415 Biología Molecular
ISSN
1422-0067
Revisión por pares
SI
Patrocinador
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)
Ministero dell’Università e della Ricerca (MUR), Prin 2022 PNRR - (project P2022YERKR)
Junta de Castilla y León, Consejería de Educación - (Grant VA033G19)
Version del Editor
Propietario de los Derechos
© 2023 The authors
Idioma
eng
Tipo de versión
info:eu-repo/semantics/publishedVersion
Derechos
openAccess
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