Biochemical properties of three plant nucleases with anticancer potential

Kód výsledku v IS VaVaI

RIV/60077344:_____/11:00357370 - isvavai.cz

Nalezeny alternativní kódy

RIV/00216208:11110/11:10303 RIV/60461373:22330/11:43870044

Výsledek na webu

http://dx.doi.org/10.1016/j.plantsci.2010.10.006

DOI - Digital Object Identifier

10.1016/j.plantsci.2010.10.006

Jazyk výsledku

angličtina

Název v původním jazyce

Biochemical properties of three plant nucleases with anticancer potential

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

Biochemical properties of three plant nucleases with anticancer potential

Popis výsledku anglicky

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.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EB - Genetika a molekulární biologie

OECD FORD obor

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Projekt

GA521/09/1214: Modifikace a produkce bifunkčních nukleáz in planta a analýza jejich protinádorových a biologických aktivit

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2011

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Plant Science

ISSN

0168-9452

e-ISSN

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Svazek periodika

180

Číslo periodika v rámci svazku

2

Stát vydavatele periodika

IE - Irsko

Počet stran výsledku

9

Strana od-do

343-351

Kód UT WoS článku

000286562200022

EID výsledku v databázi Scopus

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