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 22-nov-2024