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DNA‐nuclease activity of the single‐chain ribosome‐inactivating proteins dianthin 30, saporin 6 and gelonin
Author(s) -
Roncuzzi L.,
Gasperi-Campani A.
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00776-4
Subject(s) - ribosome inactivating protein , saporin , ricin , nuclease , immunotoxin , dna , ribosome , cleavage (geology) , chemistry , depurination , microbiology and biotechnology , biochemistry , biology , rna , toxin , gene , in vitro , cytotoxicity , paleontology , fracture (geology)
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.