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Statements

Subject Item
n2:RIV%2F60461373%3A22330%2F11%3A43870044%21RIV12-MSM-22330___
rdf:type
skos:Concept n11:Vysledek
dcterms:description
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. 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.
dcterms:title
Biochemical properties of three plant nucleases with anticancer potential Biochemical properties of three plant nucleases with anticancer potential
skos:prefLabel
Biochemical properties of three plant nucleases with anticancer potential Biochemical properties of three plant nucleases with anticancer potential
skos:notation
RIV/60461373:22330/11:43870044!RIV12-MSM-22330___
n11:predkladatel
n12:orjk%3A22330
n3:aktivita
n6:P n6:Z
n3:aktivity
P(GA521/09/1214), Z(AV0Z50510513), Z(MSM6046137305)
n3:cisloPeriodika
2
n3:dodaniDat
n10:2012
n3:domaciTvurceVysledku
n4:4654730 n4:1120530 n4:9836861 n4:1002902
n3:druhVysledku
n8:J
n3:duvernostUdaju
n15:S
n3:entitaPredkladatele
n16:predkladatel
n3:idSjednocenehoVysledku
188255
n3:idVysledku
RIV/60461373:22330/11:43870044
n3:jazykVysledku
n19:eng
n3:klicovaSlova
Anti-tumor effect; N-glycosylation; dsRNase activity; Plant nuelease I family
n3:klicoveSlovo
n7:N-glycosylation n7:dsRNase%20activity n7:Anti-tumor%20effect n7:Plant%20nuelease%20I%20family
n3:kodStatuVydavatele
IE - Irsko
n3:kontrolniKodProRIV
[9ED6AF65DE59]
n3:nazevZdroje
Plant Science
n3:obor
n20:CE
n3:pocetDomacichTvurcuVysledku
4
n3:pocetTvurcuVysledku
6
n3:projekt
n9:GA521%2F09%2F1214
n3:rokUplatneniVysledku
n10:2011
n3:svazekPeriodika
180
n3:tvurceVysledku
Lipovová, Petra Podzimek, Tomáš Šantrůček, Jiří Poučková, Pavla Spiwok, Vojtěch Matoušek, Jaroslav
n3:wos
000286562200022
n3:zamer
n5:AV0Z50510513 n5:MSM6046137305
s:issn
0168-9452
s:numberOfPages
9
n18:organizacniJednotka
22330