Isolation and characterization of two new N-glycosidase type-1 ribosome-inactivating proteins,unrelated in amino-acid sequence,fromPetrocoptis species |
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| Authors: | F Javier Arias M Angeles Rojo J Miguel Ferreras Rosario Iglesias Raquel Muñoz Fernando Soriano Enrique Méndez Luigi Barbieri Tomás Girbés |
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| Institution: | (1) Departamento de Bioquímica, Biología Molecular y Fisiología, Facultad de Ciencias, Universidad de Valladolid, E-47005 Valladolid, Spain;(2) Servicio de Endocrinología, Centro Ramón y.Cajal, Carretera de Colmenar Viejo, E-28034 Madrid, Spain;(3) Dipartimento di Patologia Sperimentale, Università di Bologna, I-40126 Bologna, Italy |
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| Abstract: | Two new N-glycosidase type-1 ribosome-inactivating proteins (RIPs), denoted petroglaucin 1 and petrograndin, respectively, were isolated from the plantsPetrocoptis glaucifolia (Lag.) Boiss sp.viscosa (Rothm.) Laínz andPetrocoptis grandiflora Rothm. These new RIPs do not share H2N-terminal amino-acid sequence homology with petroglaucin (now denoted as petroglaucin 2), the only other type-1 RIP to be isolated fromP. glaucifolia (Arias et al. (1992) Planta186, 532–540). Petroglaucin 1 shares amino-acid sequence homology with RIPs from Cucurbitaceae while petroglaucin 2 and petrograndin do so with saporins and dianthin 30 (Caryophyllaceae). The new RIPs strongly inhibited protein synthesis at subnanomolar concentrations in rabbit reticulocyte lysates and other eukaryotic cell-free systems, but they were inactive on bacterial ribosomes. |
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| Keywords: | Petrocoptis Petroglaucin Petrograndin Ribosome-inactivating protein rRNA N-glycosidase Translation (inhibition) |
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