Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.21.1 (DNase)
 7,655 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The difference in the antigenic determinant size of DNA for sera from patients with SLE and rabbit anti-DNA sera were investigated. Haptenic inhibition studies were carried out by measuring the inhibition of [3H]DNA-antibody binding by three different types of oligonucleotides which were prepared from formic acid-diphenylamine digests, hydrazinolyzed digests and pancreatic DNase digests, respectively. Oligonucleotides from DNase I digests showed potent inhibitory activity with both SLE sera and rabbit sera. However, the inhibitory activities of purine and pyrimidine oligonucleotides were more potent for SLE sera than for rabbit anti-DNA sera. The determinant size estimated for rabbit sera was in the range of tetra-to heptanucleotide, while in SLE sera it was in the range of di-and trinucleotide.
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PMID:Characteristic differences in inhibitory effects of oligodeoxyribonucleotides from DNA on human systemic lupus erythematodes (SLE) sera and rabbit anti-DNA sera. 7 86

A distinct reverse (R-) banding pattern was produced on human chromosomes by digesting chromosome spreads with pancreatic deoxyribonuclease I (DNase I) in the presence of an excess of chromomycin A3 (CMA), followed by staining with Giemsa. The banding pattern corresponds with that obtained by chromomycin A3 fluorescence, and bands which fluorescence brightly with chromomycin appear darkly with Giemsa. The same relationship was observed in two plants, Scilla siberica and Ornithogalum caudatum, which have contrasting types of heterochromatin. Chromomycin bright C-bands stained darkly with the CMA/DNase I technique, whereas chromomycin negative C-bands appeared lightly stained. The digestion patterns are thought to reflect the variation in chromomycin binding capacity along the chromosome with R-bands and dark C-bands being sites which preferentially bind the antibiotic.
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PMID:R-banding produced by DNase I digestion of chromomycin-stained chromosomes. 7 38

At various times following estrogen administration, the nuclear matrix was isolated from the liver of male Xenopus laevis by sucrose gradient centrifugation of nuclei treated with a high-salt buffer and DNase I in the presence of a proteolytic inhibitor (PMSC--phenylmethyl sulfonyl chloride). Electron micrographs of the nuclear matrix demonstrate a sponge-like network attached to a well-defined inner envelope with a ribosome-free outer envelope. Chemical analyses show that the HSB-DNase-treated nuclei consist of 16% DNA, 2% RNA, and 82% protein, a composition that is consistent with that of nuclear matrices isolated from other species. The specific activity of the matrix-associated RNA following estrogen treatment appears to be maximally enhanced after 5 h and decreases until approximately 12 h, when the activity begins to increase again.
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PMID:Isolation and characterization of the nuclear matrix from the male Xenopus laevis following estrogen administration: kinetics of [3H] uridine incorporation. 9 25

Aqueous solutions of DNA were gamma-irradiated in the presence and absence of oxygen and enzymatically hydrolysed by the combined action of pancreatic deoxyribonuclease (DNase I), snake-venom phosphodiesterase (PDE I), spleen phosphodiesterase (PDE II) and alkaline phosphatase. In contrast to unirradiated DNA, which is fully hydrolysed to nucleosides by these enzymes, gamma-irradiated DNA yields a series of oligonucleotides. Their isolation might enalbe the future identification of the chemical nature of DNA lesions.
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PMID:Enzymatic digestion of DNA gamma-irradiated in aqueous solution separation of the digests by ion-exchange chromatography. 21 Jan 33

Viable mutants of polyoma with small deletions ranging in size from 2 to 75 base pairs were obtained by infecting 3T3 cells with polyoma DNA that had been cleaved once with HaeII endonuclease or with DNase-Mn2+ digestion. The HaeII endonuclease-cleaved DNA yielded mutants with deletions at map position 72--73, whereas the mutants generated by DNase I-Mn2+ digestion had deletions either at map position 72--73 or within the map coordinates 92 and 99. Both groups of mutants appeared to grow as well as wild-type virus in 3T3 cells. The deletions at map position 72--73 did not alter the virus's ability to transform rat cells. Hence, the region just to the early side of the origin of DNA replication is not essential for vegetative growth or transformation. But the mutants with deletions in the region between map coordinates 92 and 99, a segment thought to code for polyoma large and middle T antigens (Hutchinson et al., Cell 15:65--77, 1978; Smart and Ito, Cell 15:1427--1437, 1978; Soeda et al., Cell 17:357--370, 1979), transformed rat cells at 0.2 to 0.05 the efficiency of wild-type virus.
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PMID:Construction and analysis of viable deletion mutants of polyoma virus. 22 75

The disposition of chromosome proteins about the endogenous proviral DNA of BALB-c mouse has been studied. The sensitivity of the endogenous proviral DNA sequences to deoxyribonuclease I (DNaseI) was analysed in BALB-c mouse tissues (liver and spleen) and in the cell line JLS-V9 which does not produce virus. On all of these preparations the endogenous proviral DNA was as sensitive to DNase I digestion as total chromatin. Since the proviral genes in JLS-V9 cells were silent, it was of interest to study possible changes in the chromatin structure following virus induction by iododeoxyuridine. We could not detect any increase in the sensitivity of the endogenous proviral DNA to DNase I digestion following induction. The induction was very efficient, however, since 60% of the cells responded to produce intracellular virus antigens.
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PMID:Activation of the endogenous proviral genes in mouse cells is not followed by increased sensitivity to deoxyribonuclease I digestion. 23 39

We have analyzed the DNA generated upon treatment of oviduct nuclei with pancreatic DNase I (deoxyribonucleate 3'-oligonucleotidohydrolase; EC 3.1.4.6), with cDNA copies of specific mRNA sequences to study the structure and organization of transcriptionally active genes in chromatin. In this report we examine the kinetics of digestion of three classes of genes in the oviduct which are transcribed at significantly different rates. Our results indicate that the ovalbumin genes appear to be organized by chromatin proteins in such a way that they are rendered exceedingly sensitive to digestion by DNase I. This sensitivity is not observed in the liver, a tissue in which these genes are transcriptionally inert. Furthermore, the transcriptionally inactive globin genes in the oviduct are not selectively sensitive to nuclease attack and are digested 5 times more slowly in the ovalbumin genes in this tissue. In addition, we have examined the accessibility of a complex subset of genes that are rarely represented in the mRNA and are likely to be transcribed at a frequency orders of magnitude below that of the ovalbumin gene. Comparison of the accessibility of these sequences with that of the ovalbumin gene indicates that these two subsets of genes are recognized and cleaved by DNase I at similar rates. These results suggest that the maintenance of an active conformation about specific genes does not reflect the polymerase distribution about these genes. This active conformation is therefore not confined to sequences actively engaged in the transcription process and may reflect the structure about a subpopulation of the genome which represents the transcriptional potential of a given cell type.
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PMID:Genes transcribed at diverse rates have a similar conformation in chromatin. 27 Jul 19

The DNase I (EC 3.1.21.1) sensitivity of transcribed yeast chromatin has been examined. We find that, in contrast to chromatin from higher eukaryotes, transcribed yeast chromatin and total yeast chromatin are equally sensitive to DNase I digestion. We interpret these results to mean that the entire yeast genome exists in a state that represents a restricted proportion of total chromatin in higher eukaryotes.
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PMID:Yeast chromatin is uniformly digested by DNase-I. 38 38

A deoxyribonuclease inhibitor has been purified from KB cells by chromatography on single-stranded DNA-cellulose. Polyacrylamide gel electrophoresis showed the purified preparation to contain two major polypeptides in sodium dodecyl sulfate, with molecular weights of 72,000 and 65,000, but only one major band (with a molecular weight of approximately 140,000) after electrophoresis under nondenaturing conditions. The protein inhibits the hydrolysis of single-stranded DNA by KB DNase, DNase I, DNase II, and nuclease S1, but has no effect on the hydrolysis of double-stranded DNA by these enzymes. The inhibitor causes a reduction in the rate of hydrolysis of DNA by the deoxyribonuclease, probably by reducing the effective concentration of substrate.
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PMID:A deoxyribonucleic acid binding protein from KB cells which inhibits deoxyribonuclease activity on single-stranded DNA. 42 57

Cultured mammary cells from GR mouse were used to analyse proteins associated with the mononucleosomes and released by a short micrococcal DNase treatment of nuclei. On metrizamide density gradients, mononucleosomes appear to be heterogeneous according to their content of associated non-histone proteins. Proteins associated with the denser fraction (1.22 - 1.24 g/ml) were analysed by two dimensional electrophoresis and compared to the proteins released by DNase I treatment. All the proteins associated with mononucleosomes were also released by DNase I treatment. It could then be assumed that these proteins are associated with the active part of the genome. Additional proteins were released by micrococcal DNase treatment of the nuclei. They could be involved in a higher order organization of chromatin.
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PMID:Comparison of non histone proteins selectively associated with nucleosomes with proteins released during limited DNase digestions. 44 Sep 75


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