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.
Interactions between saporin, a ribosome-inactivating protein, and DNA: A study by atomic force microscopy / Poma, A.; Spano, L.; Pittaluga, E.; Tucci, A.; Palladino, L.; Limongi, T.. - In: JOURNAL OF MICROSCOPY. - ISSN 0022-2720. - 217:1(2005), pp. 69-74. [10.1111/j.0022-2720.2005.01436.x]
|Titolo:||Interactions between saporin, a ribosome-inactivating protein, and DNA: A study by atomic force microscopy|
|Data di pubblicazione:||2005|
|Digital Object Identifier (DOI):||http://dx.doi.org/10.1111/j.0022-2720.2005.01436.x|
|Appare nelle tipologie:||1.1 Articolo in rivista|