title: Ribosome-inactivating proteins (RNA N-glycosidases) from the seeds of Saponaria ocymoides and Vaccaria pyramidata.
abstract: From the seeds of the Caryophyllaceae Saponaria ocymoides and Vaccaria pyramidata two proteins were purified which have the properties of the type-1 (single-chain) ribosome-inactivating proteins [reviewed by Barbieri, L., Battelli, M. G. & Stirpe, F. (1993) Ribosome-inactivating proteins from plants, Biochim. Biophys. Acta 1154, 237-282]. The proteins have molecular masses of 30.2 kDa (S. ocymoides) and 28.0 kDa (V. pyramidata) and pI greater than 9.5, their N-terminal amino acid sequences are similar to those of saporin-S6 and dianthin 30, ribosome-inactivating proteins from other Caryophyllaceae, and they partially cross-react with sera against these proteins. Both proteins inhibit protein synthesis by a rabbit-reticulocyte lysate with IC50 (concentrations giving 50% inhibition) below 10(-10) M, have a smaller effect on poly(U)-directed phenylalanine polymerisation by rat liver ribosomes (nanomolar IC50, approximately) and on protein synthesis by various cell lines (IC50 ranging from 4 nM to > 3000 nM) and possess rRNA N-glycosidase activity, releasing 1 mol adenine/ribosome.
authors.affiliation: Dipartimento di Patologia Sperimentale, Università di Bologna, Italy.
authors.forename: A
authors.initials: A
authors.lastname: Bolognesi
authors.forename: F
authors.initials: F
authors.lastname: Olivieri
authors.forename: M G
authors.initials: MG
authors.lastname: Battelli
authors.forename: L
authors.initials: L
authors.lastname: Barbieri
authors.forename: A I
authors.initials: AI
authors.lastname: Falasca
authors.forename: A
authors.initials: A
authors.lastname: Parente
authors.forename: F
authors.initials: F
authors.lastname: Del Vecchio Blanco
authors.forename: F
authors.initials: F
authors.lastname: Stirpe
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D006801:Humans; D007928:Lethal Dose 50; D051379:Mice; D008969:Molecular Sequence Data; D009699:N-Glycosyl Hydrolases / Q000302:isolation & purification / Q000378:metabolism / Q000494:pharmacology* / Q000633:toxicity; D010940:Plant Proteins / Q000302:isolation & purification / Q000494:pharmacology* / Q000633:toxicity; D010944:Plants / Q000196:embryology / Q000201:enzymology*; D011500:Protein Synthesis Inhibitors / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology; D051381:Rats; D054788:Ribosome Inactivating Proteins; D012270:Ribosomes / Q000187:drug effects* / Q000378:metabolism; D014407:Tumor Cells, Cultured
chemical_list: D010940:Plant Proteins; D011500:Protein Synthesis Inhibitors; D009699:N-Glycosyl Hydrolases; D054788:Ribosome Inactivating Proteins