Ribosome-inactivating proteins depurinate poly(ADP-ribosyl)ated poly(ADP-ribose) polymerase and have transforming activity for 3T3 fibroblasts |
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Authors: | Barbieri Luigi Brigotti Maurizio Perocco Paolo Carnicelli Domenica Ciani Marialibera Mercatali Laura Stirpe Fiorenzo |
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Affiliation: | Dipartimento di Patologia sperimentale, Università di Bologna, Via San Giacomo 14, I-40126 Bologna, Italy. |
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Abstract: | It has been known that ribosome-inactivating proteins (RIPs) from plants damage ribosomes by removing adenine from a precise position of rRNA. Subsequently it was observed that all tested RIPs depurinate DNA, and some of them also non-ribosomal RNAs and poly(A), hence the denomination of adenine polynucleotide glycosylases was proposed. We report now that ricin, saporin-L2, saporin-S6, gelonin and momordin depurinate also poly(ADP-ribosyl)ated poly(ADP-ribose) polymerase (auto modified enzyme), an enzyme involved in DNA repair. We observed also that all RIPs but gelonin induce transformation of fibroblasts, possibly as a consequence of damage to DNA and of the altered DNA repair system. |
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