TY - JOUR
T1 - Ribosome-inactivating proteins (RNA N-glycosidases) from the seeds of Saponaria ocymoides and Vaccaria pyramidata
AU - Bolognesi, A.
AU - Olivieri, F.
AU - Battelli, M. G.
AU - Barbieri, L.
AU - Falasca, A. I.
AU - Parente, A.
AU - Del Vecchio Blanco, F.
AU - Stirpe, F.
PY - 1995
Y1 - 1995
N2 - 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. and 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.
AB - 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. and 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.
KW - protein synthesis
KW - ribosome-inactivating protein
KW - RNA-N-glycosidase
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U2 - 10.1111/j.1432-1033.1995.tb20343.x
DO - 10.1111/j.1432-1033.1995.tb20343.x
M3 - Article
C2 - 7737197
AN - SCOPUS:0028969614
VL - 228
SP - 935
EP - 940
JO - European Journal of Biochemistry
JF - European Journal of Biochemistry
SN - 0014-2956
IS - 3
ER -