Ribosome-inactivating proteins depurinate poly(ADP-ribosyl)ated poly(ADP-ribose) polymerase and have transforming activity for 3T3 fibroblasts.
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.
Barbieri
Luigi
L
Dipartimento di Patologia sperimentale, Università di Bologna, Via San Giacomo 14, I-40126 Bologna, Italy.
Brigotti
Maurizio
M
Perocco
Paolo
P
Carnicelli
Domenica
D
Ciani
Marialibera
M
Mercatali
Laura
L
Stirpe
Fiorenzo
F
D016475:3T3 Cells; D000818:Animals; D002461:Cell Line, Transformed; D051379:Mice; D008807:Mice, Inbred BALB C; D011065:Poly(ADP-ribose) Polymerases / Q000378:metabolism*; D011506:Proteins / Q000502:physiology*; D011687:Purines / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism*
D011506:Proteins; D011687:Purines; D011065:Poly(ADP-ribose) Polymerases