RT info:eu-repo/semantics/article
T1 Structural and functional characterization of the cytotoxic protein ledodin, an atypical ribosome‐inactivating protein from shiitake mushroom (Lentinula edodes)
A1 Citores González, Lucía
A1 Ragucci, Sara
A1 Russo, Rosita
A1 Gay, Claudia C.
A1 Chambery, Angela
A1 Di Maro, Antimo
A1 Iglesias Álvarez, María del Rosario
A1 Ferreras Rodríguez, José Miguel
K1 Protein synthesis
K1 Ribosome-inactivating protein
K1 Ribotoxin
K1 rRNA N-glycosylase
K1 Shiitake
K1 Toxin
K1 24 Ciencias de la Vida
K1 2403 Bioquímica
AB We have purified ledodin, a cytotoxic 22-kDa protein from shiitake mushroom (Lentinula edodes) consisting of a 197 amino acid chain. Ledodin possessed N-glycosylase activity on the sarcin-ricin loop of mammalian 28S rRNA and inhibited protein synthesis. However, it was not active against insect, fungal and bacterial ribosomes. In vitro and in silico studies suggested that ledodin exhibits a catalytic mechanism like that of DNA glycosylases and plant ribosome-inactivating proteins. However, the sequence and structure of ledodin was not related to any protein of known function, although ledodin-homologous sequences were found in the genome of several species of fungi, some edible, belonging to different orders of the class Agaricomycetes. Therefore, ledodin could be the first of a new family of enzymes widely distributed among this class of basidiomycetes. The interest of these proteins lies both, in the fact that they can be a toxic agent of some edible mushrooms and in their application in medicine and biotechnology.
PB Wiley
SN 0961-8368
YR 2023
FD 2023
LK https://uvadoc.uva.es/handle/10324/58979
UL https://uvadoc.uva.es/handle/10324/58979
LA eng
NO Protein Science, 2023, vol. 32, n. 4, e4621
NO Producción Científica
DS UVaDOC
RD 11-jul-2024