Biochemical properties of three plant nucleases with anticancer potential
Language English Country Ireland Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
21421379
DOI
10.1016/j.plantsci.2010.10.006
PII: S0168-9452(10)00271-2
Knihovny.cz E-resources
- MeSH
- Antineoplastic Agents chemistry isolation & purification metabolism pharmacology MeSH
- Arabis enzymology MeSH
- Deoxyribonucleases chemistry isolation & purification metabolism pharmacology MeSH
- Glycosylation MeSH
- Humulus enzymology MeSH
- Hydrogen-Ion Concentration MeSH
- Humans MeSH
- Models, Molecular MeSH
- Molecular Sequence Data MeSH
- Mice, Nude MeSH
- Mice MeSH
- Cell Proliferation drug effects MeSH
- Recombinant Proteins chemistry isolation & purification metabolism pharmacology MeSH
- Ribonucleases chemistry isolation & purification metabolism pharmacology MeSH
- Plant Proteins chemistry isolation & purification metabolism pharmacology MeSH
- Amino Acid Sequence MeSH
- Sequence Alignment MeSH
- Solanum lycopersicum enzymology MeSH
- Substrate Specificity MeSH
- Nicotiana enzymology genetics MeSH
- Temperature MeSH
- Animals MeSH
- Check Tag
- Humans MeSH
- Mice MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Antineoplastic Agents MeSH
- Deoxyribonucleases MeSH
- Recombinant Proteins MeSH
- Ribonucleases MeSH
- Plant Proteins MeSH
Biochemical and structural properties of three recombinant (R), highly homologous, plant bifunctional nucleases from tomato (R-TBN1), hop (R-HBN1) and Arabis brassica (R-ABN1) were determined. These nucleases cleave single- and double-stranded substrates, as well as both RNA and DNA with nearly the same efficiency. In addition, they are able to cleave several artificial substrates and highly stable viroid RNA. They also possess 3'-nucleotidase activity; therefore, they can be classified as nuclease I family members. Interestingly, poly(G) is resistant to cleavage and moreover it inhibits dsDNase, ssDNase and RNase activity of the studied nucleases. All three nucleases exhibit zinc-dependence and a strong stimulatory effect of Zn²+ for dsDNA cleavage. 3-D models, predicted on the basis of experimental structure of P1 nuclease, show nine amino acid residues responsible for interactions with zinc atoms, located in the same positions as in P1 nuclease. It was also shown that R-TBN1, R-HBN1, and R-ABN1 are all N-glycosylated. Oligosaccharidic chains constitute about 16% of their MW. In addition, an anticancer potential of the R-ABN1 is compared in this work with previously tested R-TBN1, and R-HBN1. R-ABN1 injected intravenously showed 70% inhibitory effect on growth of human prostate carcinoma in athymic mice.
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