2026-05-05T21:02:56Zhttps://uvadoc.uva.es/oai/request

oai:uvadoc.uva.es:10324/589792023-04-24T19:00:46Zcom_10324_1134com_10324_931com_10324_894col_10324_1213

00925njm 22002777a 4500 dc Citores González, Lucía author Ragucci, Sara author Russo, Rosita author Gay, Claudia C. author Chambery, Angela author Di Maro, Antimo author Iglesias Álvarez, María del Rosario author Ferreras Rodríguez, José Miguel author 2023 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. Protein Science, 2023, vol. 32, n. 4, e4621 0961-8368 https://uvadoc.uva.es/handle/10324/58979 10.1002/pro.4621 Protein Science 1469-896X Structural and functional characterization of the cytotoxic protein ledodin, an atypical ribosome‐inactivating protein from shiitake mushroom (Lentinula edodes)