Ribosome-inactivating proteins depurinate poly(ADP-ribosyl)ated poly(ADP-ribose) polymerase and have transforming activity for 3T3 fibroblasts

Luigi Barbieri, Maurizio Brigotti, Paolo Perocco, Domenica Carnicelli, Marialibera Ciani, Laura Mercatali, Fiorenzo Stirpe

Research output: Contribution to journal › Article › peer-review

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.

Original languageEnglish
Pages (from-to)178-182
Number of pages5
JournalFEBS Letters
Volume538
Issue number1-3
DOIs
Publication statusPublished - Mar 13 2003

Keywords

  • Adenine polynucleotide glycosylase
  • Cell transformation
  • Poly(ADP-ribose) polymerase
  • Ribosome-inactivating protein

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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