RT info:eu-repo/semantics/article
T1 Isolation, characterization and biological action of type-1 ribosome-inactivating proteins from tissues of Salsola soda L.
A1 Landi, Nicola
A1 Ragucci, Sara
A1 Citores González, Lucía
A1 Clemente, Angela
A1 Hussain, Hafiza Z. F.
A1 Iglesias Álvarez, María del Rosario
A1 Ferreras Rodríguez, José Miguel
A1 Di Maro, Antimo
K1 Toxicology
K1 Proteins - Synthesis
K1 Ribosomes - Structure
K1 Proteínas - Síntesis
K1 Molecular biology
K1 Plant Sciences
K1 Plantas comestibles
K1 Biochemistry
K1 Proteins - Purification
K1 RNA
K1 ARN
K1 Antifungal agents
K1 Salsola soda
K1 Cytotoxicity
K1 Citotoxicidad
K1 2302.27 Proteínas
K1 2302 Bioquímica
K1 2415 Biología Molecular
AB Ribosome-inactivating proteins (RIPs) are known as RNA N-glycosylases. They depurinate the major rRNA, damaging ribosomes and inhibiting protein synthesis. Here, new single-chain (type-1) RIPs named sodins were isolated from the seeds (five proteins), edible leaves (one protein) and roots (one protein) of Salsola soda L. Sodins are able to release Endo’s fragment when incubated with rabbit and yeast ribosomes and inhibit protein synthesis in cell-free systems (IC50 = 4.83–79.31 pM). In addition, sodin 5, the major form isolated from seeds, as well as sodin eL and sodin R, isolated from edible leaves and roots, respectively, display polynucleotide:adenosine glycosylase activity and are cytotoxic towards the Hela and COLO 320 cell lines (IC50 = 0.41–1200 nM), inducing apoptosis. The further characterization of sodin 5 reveals that this enzyme shows a secondary structure similar to other type-1 RIPs and a higher melting temperature (Tm = 76.03 ± 0.30 °C) and is non-glycosylated, as other sodins are. Finally, we proved that sodin 5 possesses antifungal activity against Penicillium digitatum.
PB MDPI
SN 2072-6651
YR 2022
FD 2022
LK https://uvadoc.uva.es/handle/10324/61139
UL https://uvadoc.uva.es/handle/10324/61139
LA eng
NO Toxins, 2022, Vol. 14, Nº. 8, 566
NO Producción Científica
DS UVaDOC
RD 07-ago-2024