Abstract
The single-chain ribosome-inactivating proteins (sc-RIPs) from plant origin are antiviral and antiproliferative agents employed in the preparation of immunotoxins, Similarly to the A-chains of ricin, sc-RIPs act as rRNA N-glycosidases. We demonstrate here that dianthin 30, saporin 6 and gelonin exert a specific nuclease activity on supercoiled DNA. Four specific sites of cleavage introduced by dianthin 30 and by saporin 6 and two specific sites of cleavage introduced by gelonin have been identified and mapped in pBR322.
| Original language | English |
|---|---|
| Pages (from-to) | 16-20 |
| Number of pages | 5 |
| Journal | FEBS Letters |
| Volume | 392 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - Aug 19 1996 |
Keywords
- Dianthin 30
- DNAse activity
- Gelonin
- Ribosome-inactivating protein
- Saporin 6
- Supercoiled DNA
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
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Roncuzzi, L., & Gasperi-Campani, A. (1996). DNA-nuclease activity of the single-chain ribosome-inactivating proteins dianthin 30, saporin 6 and gelonin. FEBS Letters, 392(1), 16-20. https://doi.org/10.1016/0014-5793(96)00776-4