Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.1.22.1 (DNase II)
429 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Deoxyribonucleases from eggs and the liver of Xenopus laevis were partially purified by DEAE-cellulose and heparin-Sepharose affinity column chromatographies. The fractions having egg and liver DNase activities were eluted on high performance liquid chromatography through TSK gel G3000SW at the molecular weights of 41.5 and 45 kDa, respectively. The frog DNases hydrolyzed a native DNA over a heat-denatured DNA, and also formed double-strand cuts not only in linear lambda-DNA but also in closed circular pBR322DNA. The pH optimum of the DNases was 4.5-5.0 in 50 mM acetate buffer. These enzyme activities were abolished by treatment at 80 degrees C for 5 min and pH 2, 3 or 12 for 1 h. The enzymes act in such a manner as deoxyribonuclease II (from bovine spleen)-type nuclease with respect to substrate specificity, optimum pH and cation dependence.
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PMID:[Partial purification and properties of deoxyribonucleases from eggs and liver of Xenopus laevis. Comparison with deoxyribonuclease II from bovine spleen]. 816 69

We have used hydroxy-radical and deoxyribonuclease-I footprinting to probe the interaction of mithramycin with DNA fragments containing the sequences (AT)10X(AT)10 (X = CCCG, CCGC or CGGC) and A14GCCCT15. As expected the drug produces clear footprints located around the central four GC base pairs. The exact position of the footprint is different for the four sequences; the footprint with CCCG is displayed by two base pairs in the 5' direction relative to GCCC. These variations are explained by suggesting that mithramycin avoids the dinucleotide CG and binds better to GG/CC than GC. Although there is little change in deoxyribonuclease-I cleavage of the surrounding blocks of (AT)n, cleavage by deoxyribonuclease II is markedly enhanced and certain thymines on the 5' side of the ligand-binding site become hyperreactive to hydroxy-radical attack. Adjacent regions of An.Tn show enhanced rates of deoxyribonuclease-I cleavage in the presence of the antibiotic.
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PMID:DNA-sequence binding preference of the GC-selective ligand mithramycin. Deoxyribonuclease-I/deoxyribonuclease-II and hydroxy-radical footprinting at CCCG, CCGC, CGGC, GCCC and GGGG flanked by (AT)n and An.Tn. 839 9

Cell death occurs by apoptosis during programmed deletion of cells and following exposure to cytotoxic agents. Central to the mechanism of apoptosis is internucleosomal DNA digestion by an endogenous endonuclease which is thought to mediate cell death. An axiom of apoptosis is that the endonuclease involved is a Ca2+/Mg(2+)-dependent endonuclease. During purification of endonucleases from Chinese hamster ovary cells, we found little Ca2+/Mg(2+)-dependent endonuclease activity, but large amounts of an endonuclease active below pH 7. This acidic endonuclease was activated in intact cells by reducing intracellular pH values below 7 with a proton ionophore. This activity generated internucleosomal digestion of DNA characteristic of apoptosis. Nuclear extracts contained a cation-independent endonuclease with identical pH-dependent activity. We have compared the acidic endonuclease to bovine deoxyribonuclease II (DNase II) and have found them nearly identical by all tests, including sensitivity to various inhibitors, purification by the same chromatographic steps, and recognition by antibody raised against the bovine enzyme. Addition of either the acidic endonuclease or bovine DNase II to isolated nuclei induced internucleosomal DNA digestion up through pH 6.5. These data demonstrate that DNase II can mediate internucleosomal DNA digestion characteristic of apoptosis following intracellular acidification. Furthermore, these data question the premise that the Ca2+/Mg(2+)-dependent endonuclease is the only endonuclease involved in apoptosis.
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PMID:Identification of deoxyribonuclease II as an endonuclease involved in apoptosis. 842 78

Vertebrate telomeres contain arrays of nucleosomes with unusually short and regular repeat lengths (Makarov, V. L., Lejnine, S., Bedoyan, J., and Langmore, J. P.(1993) Cell 73, 775-787; Lejnine, S., Makarov, V., and Langmore, J. P. (1995) Proc. Natl. Acad. Sci. U. S. A. 92, 2393-2397). In order to better define the specific structural features of telomere chromatin, we examined the condensation and H1 content of telomere nucleoproteins from rat liver. Velocity sedimentation analysis shows that telomeric nucleosome arrays condense with increasing ionic strength and molecular weight in a manner comparable with that of bulk chromatin despite the very short repeat length. However, these condensed structures do not exhibit the approximately 100-base pair deoxyribonuclease II repeat characteristic of condensed bulk chromatin. Frictional coefficient calculations suggest that telomere-specific higher order structure is more compact than bulk chromatin. Nucleoprotein gel electrophoresis shows that telomeric dinucleosomes from soluble chromatin contain H1. Finally, direct isolation and analysis of telomere nucleoproteins from formaldehyde-cross-linked nuclei indicate the presence of core histone proteins and H1. These results are consistent with the view that a major fraction of the long telomeres of rat are organized as specialized nucleosome arrays with features similar but not identical to those of bulk chromatin.
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PMID:Condensation of rat telomere-specific nucleosomal arrays containing unusually short DNA repeats and histone H1. 870 94

Research into the use of new genetic markers is difficult and costly, but it is necessary for more accurate criminal individualization and paternity testing as well as for analysis of genetic diseases. Recently, we discovered that human ribonuclease (RNase), deoxyribonuclease I (DNase I) and deoxyribonuclease II (DNase II) are characteristic markers showing genetic polymorphism and useful for forensic investigation. DNase I is particularly well suited to practical use, since it shows a well-balanced gene frequency, a high concentration in several body fluids (blood, sweat, urine, breast milk and semen) and tissues (pancreas, liver and kidney), stability against severe conditions (exposure of test samples to high temperature, high humidity and long-term storage), and easy and accurate detectability.
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PMID:[Discovery of genetic polymorphism of human nucleases]. 895 29

A rapid amplification of cDNA ends method, using degenerate oligonucleotides based upon the N-terminal amino acid sequence of human hepatic deoxyribonuclease II (DNase II), allowed a novel cDNA encoding DNase II to be constructed from thyroid gland RNA. The composite nucleotide sequence (1593 bases) included an open reading frame of 1080 bases, which encoded a single polypeptide of 360 amino acids (signal peptide, 16; propeptide, 91; mature protein, 253). Although the sequence of DNase II showed no significant homology to other mammalian proteins, its cDNA structural organization resembled those of the lysosomal cathepsin families. The two parts of the cDNA corresponding to the propeptide and the mature protein were expressed in Escherichia coli, and the recombinant polypeptides thus obtained were strongly stained with an anti-DNase II antibody on Western blotting. DNase II is ubiquitously expressed in human tissues, and the DNase II gene (DNASE2) was assigned to chromosome 19.
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PMID:Molecular cloning of the cDNA encoding human deoxyribonuclease II. 944 63

Recently obtained information on the cDNA encoding human deoxyribonuclease II (DNase II) (T. Yasuda et al., 1998, J. Biol. Chem. 273, 2610-2616) has made it possible to demonstrate the precise position of the the human DNase II gene (DNASE2) on human chromosomes. Two different sets of oligonucleotide primers specific for human DNase II cDNA sequences were used to amplify unique DNA fragments in the human DNase II gene from a panel of human x rodent hybrid cell lines carrying different human chromosomes. Based on this analysis, DNASE2 was assigned to human chromosome 19. Furthermore, regional localization of the gene to 19p13.2-p13.1 was achieved by fluorescence in situ hybridization analysis using a full-length cDNA probe corresponding to the entire open reading frame.
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PMID:Chromosomal localization of a human deoxyribonuclease II gene (DNASE2) to 19p13.2-p13.1 using both the polymerase chain reaction and fluorescence in situ hybridization analysis. 953 49

This review describes several types of genetic polymorphism, which have recently been identified in human urine in our laboratory, and have also been found in other human body fluids such as blood, saliva and semen. These include uropepsinogen, ribonuclease, deoxyribonuclease I (DNase I), deoxyribonuclease II (DNase II), 43-kDa glycoprotein, alpha-L-fucosidase, glutamate pyruvate transaminase, alpha-2-HS-glycoprotein, transferrin and vitamin D-binding protein. Several substances can be detected more easily in urine than in plasma. The concentrations of uropepsinogen, DNase I and DNase II in blood plasma are too low for analysis, whereas those in urine are high enough for easy typing. In practice, DNase I-polymorphism is one of the most useful genetic markers for practical purposes, because of its higher content in various body fluids including urine, a well-balanced gene frequency, and its easy and accurate detectability. Furthermore, several genetic markers previously identified in blood and/or other forensic samples can be phenotyped reproducibly and easily from the corresponding urine samples. Thus, urine, in addition to the convenience and non-invasive nature of its collection, is by no means inferior to blood as a sample source for typing in the field of forensic science. Biochemical and serological typing of genetic polymorphisms present in human urine could offer useful information to practising forensic biologists for forensic individualization of urine samples.
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PMID:Genetic polymorphisms detectable in human urine: their application to forensic individualization. 954 53

We have previously implicated deoxyribonuclease II (DNase II) as an endonuclease responsible for DNA digestion during apoptosis. The full-length human cDNA has now been cloned. The cDNA contains an open reading frame of 1078 bases coding for a 40-kDa protein. This protein is 10 kDa larger than commercially supplied enzyme, which has been proteolytically cleaved at an internal aspartate residue. The gene is located at chromosome 19p13.2, and has no significant homology to other human proteins, but has >30% identity to three predicted genes in Caenorhabditis elegans. To determine whether overexpression of DNase II induces apoptosis in Chinese hamster ovary cells, the cDNA was cotransfected with a plasmid encoding green fluorescent protein. Within 24 h, a significant proportion of green fluorescent protein-positive cells contained condensed chromatin, whereas vector-only controls remained viable. Considering that DNase II is normally active only at low pH, it was surprising that transfection induced chromatin condensation. To confirm that transfection was not activating another endonuclease, cells were incubated with the caspase inhibitor benzyloxycarbonyl-Val-Ala-Asp-(O-methyl)-fluoromethylketone; this failed to inhibit chromatin condensation induced by DNase II. These results demonstrate that DNase II acts downstream of caspase activation and that it may be activated by an as yet unknown mechanism to induce DNA digestion during apoptosis.
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PMID:The cloning and expression of human deoxyribonuclease II. A possible role in apoptosis. 981 84

The structure of the human gene for deoxyribonuclease II (DNase II; EC 3.1.22.1) was determined using several specific primers based on the human DNase II cDNA sequence [Yasuda et al. (1998). J. Biol. Chem. 273, 2610-2616] in a polymerase chain reaction-based strategy. The gene spanned about 6 kb and consisted of 6 exons. No canonical TATA or CAAT boxes could be identified within the 1341 nucleotides upstream of the putative transcription start site, although the 5'-flanking region contained a CpG island and several putative binding motifs for transcription factors Sp1 and ETF. These properties indicate that the DNase II gene is a housekeeping gene and this is compatible with its ubiquitous expression in human tissues. Three different cleavage/polyadenylation sites were identified in the 3'-flanking region, leading to the production of multiple DNase II mRNA species. However, a comparison of the entire translated sequences of the gene from a pair of subjects with homozygous DNase II phenotypes H and L revealed no differences in the nucleotide sequences.
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PMID:Structure and organization of the human deoxyribonuclease II (DNase II) gene. 992 8


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