Interactions between saporin, a ribosome-inactivating protein, and DNA: A study by atomic force microscopy

Anna Poma*, L. Spanò, E. Pittaluga, A. Tucci, L. Palladino, Tania Limongi

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

Abstract

Saporins are enzymes belonging to the PNAG class (polynucleotide: adenosine glycosidase), plant enzymes commonly known as ribosome-inactivating proteins (RIP), as a result of their property of irreversibly damaging eukaryotic ribosomes. Direct imaging with tapping-mode atomic force microscopy (AFM) has been used to study pGEM-4Z plasmid DNA binding to the saporin-SO6 (isoform from Saponaria officinalis seeds). Saporin wrapped the plasmidic DNA, and distribution of the enzyme molecules along the DNA chain was markedly variable; plasmid digested with saporin-SO6 appeared fragmented or topologically modified. The supercoiled DNA strands were cleaved, giving rise to a linearized form and to relaxed forms. Electrophoretic analysis of the effect of standard preparations of saporin-SO6 on pGEM-4S confirmed the presence of DNA strand-cleaving activity.

Original languageEnglish (US)
Pages (from-to)69-74
Number of pages6
JournalJournal of Microscopy
Volume217
Issue number1
DOIs
StatePublished - Jan 1 2005

Keywords

  • AFM
  • Polynucleotide: adenosine glycosidase (PNAG)
  • Ribosome-inactivating proteins
  • Saporin
  • pGEM-4Z

ASJC Scopus subject areas

  • Instrumentation

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