endonuclease Vs are inosine-specific nucleases that cleave at the second phosphodiester bond 3' to inosine. The human enzyme is most active towards ssRNA but is much less active towards other substrates
endonuclease Vs are inosine-specific nucleases that cleave at the second phosphodiester bond 3' to inosine. The human enzyme is most active towards ssRNA but is much less active towards other substrates
the human endonuclease V ribonuclease is specific for inosine-containing RNA, it preferentially binds to RNA and efficiently hydrolyses the second phosphodiester bond located 3' to the inosine in unpaired inosine-containing ssRNA regions in dsRNA, at 5'-IIUI-3' and 5'-UIUU-3'. But hEndoV can also cleave ssDNA substrates containing deoxyinosine. RNA is preferred to DNA by the enzyme as a substrate
the human endonuclease V ribonuclease is specific for inosine-containing RNA, it preferentially binds to RNA and efficiently hydrolyses the second phosphodiester bond located 3' to the inosine in unpaired inosine-containing ssRNA regions in dsRNA, at 5'-IIUI-3' and 5'-UIUU-3'. But hEndoV can also cleave ssDNA substrates containing deoxyinosine. RNA is preferred to DNA by the enzyme as a substrate
32P-labelled 30mer ssDNA containing deoxyinosine and/or 21mer ssRNA containing inosine are used as substrates, as well as 32P-labelled 30mer ssDNA containing deoxyinosine
32P-labelled 30mer ssDNA containing deoxyinosine and/or 21mer ssRNA containing inosine are used as substrates, as well as 32P-labelled 30mer ssDNA containing deoxyinosine
single-stranded deoxyinosine-containing DNA (5'-GCTCGGCTICGGACCGAG-3') and inosine-containing RNA (5'-CUGACUICGGAUCAGGGCC-3') oligonucleotides are synthesized and used as substrates. Substrate-recognition specificity, overview
single-stranded deoxyinosine-containing DNA (5'-GCTCGGCTICGGACCGAG-3') and inosine-containing RNA (5'-CUGACUICGGAUCAGGGCC-3') oligonucleotides are synthesized and used as substrates. Substrate-recognition specificity, overview
endonuclease Vs are inosine-specific nucleases that cleave at the second phosphodiester bond 3' to inosine. The human enzyme is most active towards ssRNA but is much less active towards other substrates
endonuclease Vs are inosine-specific nucleases that cleave at the second phosphodiester bond 3' to inosine. The human enzyme is most active towards ssRNA but is much less active towards other substrates
the human endonuclease V ribonuclease is specific for inosine-containing RNA, it preferentially binds to RNA and efficiently hydrolyses the second phosphodiester bond located 3' to the inosine in unpaired inosine-containing ssRNA regions in dsRNA, at 5'-IIUI-3' and 5'-UIUU-3'. But hEndoV can also cleave ssDNA substrates containing deoxyinosine. RNA is preferred to DNA by the enzyme as a substrate
the human endonuclease V ribonuclease is specific for inosine-containing RNA, it preferentially binds to RNA and efficiently hydrolyses the second phosphodiester bond located 3' to the inosine in unpaired inosine-containing ssRNA regions in dsRNA, at 5'-IIUI-3' and 5'-UIUU-3'. But hEndoV can also cleave ssDNA substrates containing deoxyinosine. RNA is preferred to DNA by the enzyme as a substrate
Incomplete complementation of the DNA repair defect in cockayne syndrome cells by the denV gene from bacteriophage T4 suggests a deficiency in base excision repair.
Immunosuppressive function of hepatitis B antigens in vitro: role of endoribonuclease V as one potential trans inactivator for cytokines in macrophages and human hepatoma cells.
Microinjection of Escherichia coli UvrA, B, C and D proteins into fibroblasts of xeroderma pigmentosum complementation groups A and C does not result in restoration of UV-induced unscheduled DNA synthesis.
Microinjection of T4 endonuclease V produced by a synthetic denV gene stimulates unscheduled DNA synthesis in both xeroderma pigmentosum and normal cells.
Partial complementation of the DNA repair defects in cells from xeroderma pigmentosum groups A, C, D and F but not G by the denV gene from bacteriophage T4.
the enzyme preserves the general RNase H-like structure, especially in the wedge motif, the metal-binding site and the hypoxanthine-binding pocket. The human enzyme also features several extra insertions and a characteristic four cysteine motif, in which Cys227 and Cys228, two cysteines that are highly conserved in higher eukaryotes, play important roles in catalysis
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged truncated enzyme mutant hEndoV-SF, sitting drop vapour diffusion method, mixing of 10 mg/ml protein in 20 mM Tris-HCl, pH 8.5, 300 mM NaCl, is mixed with 19% PEG 3350, 0.2 M sodium formate, 0.1 M Tris-HCl pH 7.5, or with 1.4 M ammonium sulfate, 0.2 M sodium acetate, 0.1 M Tris-HCl pH 7.5, as crystallization solution, method screening and optimization, 25°C, 2-3 days, X-ray diffraction structure determination and analysis at 2.3 a resolution
construction of truncated enzyme version representing residues Thr13-Ser250, i.e. hEndoV-SF. The mutant shows reduced enzyme activity compared to the wild-type full-length enzyme
construction of truncated enzyme version representing residues Thr13-Ser250, i.e. hEndoV-SF. The mutant shows reduced enzyme activity compared to the wild-type full-length enzyme
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, heparin affinity chromatography, and gel filtration
recombinant expression of C-terminally FLAG-V5-His6-tagged enzyme in HEK293 cell, recombinant expression of N-terminally GST-tagged wild-type and mutant enzymes in Escherichia coli