Nicking activity on pBR322 DNA of ribosome inactivating proteins from Phytolacca dioica L. leaves
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Serena Aceto
Abstract
Ribosome-inactivating proteins isolated from Phytolacca dioica L. leaves are rRNA-N-glycosidases, as well as adenine polynucleotide glycosylases. Here we report that some of them cleave supercoiled pBR322 dsDNA, generating relaxed and linear molecules. PD-L1, the glycosylated major form isolated from the winter leaves of adult P. dioica plants, produces both free 3′-OH and 5′-P termini randomly distributed along the DNA molecule, as suggested by labelling experiments with [α-32P]dCTP and [γ-32P]dATP. Moreover, when the reaction is carried out under low-salt conditions, cleavage is observed mainly at a specific site, located downstream of the ampicillin resistance gene (close to position 3200), ending with the deletion of a fragment of approximately 70 nucleotides. This cleavage pattern is similar to that obtained under the same conditions with mung bean nuclease, a single-strand endonuclease. Furthermore, pBR322 DNA treated with PD-L1 shows reduced transforming activity with E. coli HB101 competent cells in comparison to untreated control plasmid DNA.
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© by Walter de Gruyter Berlin New York
Articles in the same Issue
- Supplementary material to the paper “The connexin gene family in mammals”
- Nicking activity on pBR322 DNA of ribosome inactivating proteins from Phytolacca dioica L. leaves
- Identification of three novel mutations in the dihydropyrimidine dehydrogenase gene associated with altered pre-mRNA splicing or protein function
- The connexin gene family in mammals
- Hydrogen peroxide causes greater oxidation in cellular RNA than in DNA
- Homology modeling and SAR analysis of Schistosoma japonicum cathepsin D (SjCD) with statin inhibitors identify a unique active site steric barrier with potential for the design of specific inhibitors
- Interpretation of the reactivity of peroxidase compound II with phenols and anilines using the Marcus equation
- P. falciparum pro-histoaspartic protease (proHAP) protein peptides bind specifically to erythrocytes and inhibit the invasion process in vitro
- The snake venom metalloproteases berythractivase and jararhagin activate endothelial cells
- Visualisation of transforming growth factor-β1, tissue kallikrein, and kinin and transforming growth factor-β receptors on human clear-cell renal carcinoma cells
- cDNA cloning and heterologous expression of a wheat proteinase inhibitor of subtilisin and chymotrypsin (WSCI) that interferes with digestive enzymes of insect pests
- Proteolytic susceptibility of the serine protease inhibitor trappin-2 (pre-elafin): evidence for tryptase-mediated generation of elafin
- Labelling of four distinct trophozoite falcipains of Plasmodium falciparum by a cystatin-derived probe
Articles in the same Issue
- Supplementary material to the paper “The connexin gene family in mammals”
- Nicking activity on pBR322 DNA of ribosome inactivating proteins from Phytolacca dioica L. leaves
- Identification of three novel mutations in the dihydropyrimidine dehydrogenase gene associated with altered pre-mRNA splicing or protein function
- The connexin gene family in mammals
- Hydrogen peroxide causes greater oxidation in cellular RNA than in DNA
- Homology modeling and SAR analysis of Schistosoma japonicum cathepsin D (SjCD) with statin inhibitors identify a unique active site steric barrier with potential for the design of specific inhibitors
- Interpretation of the reactivity of peroxidase compound II with phenols and anilines using the Marcus equation
- P. falciparum pro-histoaspartic protease (proHAP) protein peptides bind specifically to erythrocytes and inhibit the invasion process in vitro
- The snake venom metalloproteases berythractivase and jararhagin activate endothelial cells
- Visualisation of transforming growth factor-β1, tissue kallikrein, and kinin and transforming growth factor-β receptors on human clear-cell renal carcinoma cells
- cDNA cloning and heterologous expression of a wheat proteinase inhibitor of subtilisin and chymotrypsin (WSCI) that interferes with digestive enzymes of insect pests
- Proteolytic susceptibility of the serine protease inhibitor trappin-2 (pre-elafin): evidence for tryptase-mediated generation of elafin
- Labelling of four distinct trophozoite falcipains of Plasmodium falciparum by a cystatin-derived probe
