Direct evidence for the deoxyribonuclease activity of the plant ribosome inactivating protein gelonin.
Several plant ribotoxins, including gelonin, were reported to have additional weak nuclease activities on supercoiled DNA. The potential contribution of this activity to their cytotoxicity has not been given serious consideration due to concerns about contaminating nucleases in the protein preparations. We now report the degradation of single-stranded DNA by preparations of native plant gelonin and recombinant gelonin produced in E. coli. The DNase activity of both preparations is similarly modulated by zinc. An SDS-PAGE DNase assay identifies gelonin as the polypeptide responsible for deoxyribonuclease activity.
Nicolas
E
E
Department of Pathology, Anatomy and Cell Biology, Jefferson Medical College, Philadelphia, PA 19107, USA.
Beggs
J M
JM
Haltiwanger
B M
BM
Taraschi
T F
TF
D004277:DNA, Single-Stranded / Q000187:drug effects; D003851:Deoxyribonucleases / Q000378:metabolism*; D010940:Plant Proteins / Q000378:metabolism* / Q000494:pharmacology; D010944:Plants / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism / Q000494:pharmacology; D054789:Ribosome Inactivating Proteins, Type 1; D012270:Ribosomes / Q000187:drug effects
D004277:DNA, Single-Stranded; D010940:Plant Proteins; D011994:Recombinant Proteins; D054789:Ribosome Inactivating Proteins, Type 1; C025674:GEL protein, Gelonium multiflorum; D003851:Deoxyribonucleases