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 | |
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Data di pubblicazione: | 2005 | |
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Digital Object Identifier (DOI): | http://dx.doi.org/10.1111/j.0022-2720.2005.01436.x | |
Appare nelle tipologie: | 1.1 Articolo in rivista |
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http://hdl.handle.net/11583/2852808