Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.22.1 (DNase II)
 429 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

It was revealed by means of nucleoprotein-celite-chromatography that DNA-protein interactions in the chromatin fraction sensitive to micrococcal nuclease and DNase II are weaker that in the resistant one. The micrococcal nuclease destroys the DNA-matrix bond resistant to salt-urea, while DNase II does not change the DNA-matrix integrity. Tightness of the DNA-protein interactions is weakened by the increasing chromatin fragmentation, but does not depend on the size of chromatin particles.
Mol Gen Mikrobiol Virusol 1988 Oct
PMID:[Stability of DNA-protein interactions in chromatin fractions with different sensitivity to nucleases]. 323 Dec 30

The activation of DNase I by Mg, Mn, Co, Ni, Fe, Cd, Zn, Ba, Sr, Ca, and Cu ions has been studied by several methods, at different pH and salt concentrations. Mg, Mn, and Co are the best activators for initial stages of degradation. A synergistic effect is shown only by the pair Mg-Ca. Optimal pH of action is always situated at 6.5. DNase II is activated to about the same degree by alkaline earths and Mn ions. Cd and Cu are strong inhibitors. Optimal pH is always 4.6. By titration of liberated secondary phosphate groups, two stages in the hydrolysis of DNA by DNase I are evidenced: a rapid phase activated most by Mg and a slow phase activated by Ca. Some possible mechanisms of action of both enzymes are outlined and the general influence of metal ions is discussed.
J Gen Physiol 1962 Mar
PMID:Activation of deoxyribonucleases by divalent cations. 1388 71

The 266 kbp genome sequence of plaque-purified, tissue culture-adapted, attenuated European Fowlpox virus FP9 has been determined and compared with the 288 kbp sequence of a pathogenic US strain (FPVUS). FP9 carries 244 of the 260 reported FPVUS ORFs (both viruses also have an unreported orthologue of conserved poxvirus gene A14.5L). Relative to FPVUS, FP9 differed by 118 mutations (26 deletions, 15 insertions and 77 base substitutions), affecting FP9 equivalents of 71 FPVUS ORFs. To help to identify mutations involved in adaptation and attenuation, the virulent parent of FP9, HP1, was sequenced at positions where FP9 differed from FPVUS. At 68 positions, FP9 and HP1 sequences were identical, reflecting differences between American and European lineages. Mutations at the remaining 50 positions in FP9 relative to FPVUS and HP1, involving 46 ORFs, therefore accounted for adaptation and attenuation. ORFs deleted during passage included those encoding members of multigene families: 12 ankyrin repeat proteins, three C-type lectin-like proteins, two C4L/C10L-like proteins, one G-protein coupled receptor protein, one V-type Ig domain protein, two N1R/p28 proteins and one EFc family protein. Tandem ORFs encoding Variola virus B22R orthologues were fused by a 5.8 kbp deletion. Single-copy genes disrupted or deleted during passage included those encoding a homologue of murine T10, a conserved DNA/pantothenate metabolism flavoprotein, photolyase, the A-type inclusion protein and an orthologue of vaccinia A47L. Gene assignments have been updated for DNase II/DLAD, binding proteins for IL-18 and interferon-gamma, phospholipid hydroperoxide glutathione peroxidase (PHGPX/GPX-4) and for a highly conserved homologue of ELOVL4.
J Gen Virol 2004 Feb
PMID:Comparison of the genome sequence of FP9, an attenuated, tissue culture-adapted European strain of Fowlpox virus, with those of virulent American and European viruses. 1476 88

Mitochondrial DNA (mtDNA) of the yeast Saccharomyces cerevisiae is organized to form mitochondrial nucleoids (mt-nucleoids) by association with specific proteins. The sensitivity of DNA-protein complexes to nuclease digestion is a useful means for examining DNA packaging and organization. However, the mt-nucleoids isolated from wild-type cells of S. cerevisiae demonstrated a significant amount of endogenous nuclease activity. In order to minimize the nuclease activity associated with the isolated mt-nucleoids, we isolated the mt-nucleoids from a mutant strain that lacked the mitochondrial nuclease, Nuc1p. In this manner, we succeeded in isolating mt-nucleoids that showed a low level of the nuclease activity. Micrococcal nuclease treatment of these mt-nucleoids led to the continuous digestion of mtDNA in the presence of Ca(2+) ions. MtDNA in the mt-nucleoids also showed the continuous digestion pattern when treated with DNase II. These results suggest that mtDNA in the mt-nucleoids is protected from nuclease digestion by association with proteins, but the organization of the mtDNA-protein complexes is different from that of nuclear chromatin, in which the unit of DNA packaging is regularly repeated.
J Gen Appl Microbiol 2008 Dec
PMID:Use of the nuc1 null mutant for analysis of yeast mitochondrial nucleoids. 1916 74

A procedure is described for the purification of salmon testis deoxyribonuclease II by means of acid extraction, fractional precipitation with ammonium sulfate, heat denaturation of extraneous proteins, and ethanol fractionation. This process separates the deoxyribonuclease activity from that of ribonuclease, phosphatase, phosphodiesterase, and protease. Over 50 per cent of the activity is retained with an over-all enrichment of 20,000-fold. The enzyme degrades both native and heat-denatured DNA, but the rate of degradation of the latter is only one-tenth that of the former. It does not hydrolyze apurinic acid. The enzyme is most stable in the pH range 4 to 5. Electrolytes are essential for the expression of its activity: monovalent ions satisfy the requirement, but divalent ones are much more effective. Above a certain optimum concentration, each electrolyte is inhibitory. The pH of maximal activity, under conditions of optimal ionic strength, is 4.8; the temperature optimum is near to 55 degrees C.
J Gen Physiol 1962 Mar 01
PMID:Deoxyribonuclease from Salmon Testes : I. Purification and properties. 1987 45

The aim of the study was to evaluate the effect of melatonin on oxidative stress, DNA fragmentation, apoptsis and proliferation in thymus tissue of rats exposed to microwaves. Wistar rats were divided in four groups: I - treated with saline; II - treated with melatonin; III - microwaves exposed; IV - microwaves exposed and melatonin treated. Melatonin (2 mg/kg i.p.) was administered daily. Animals were sacrificed after 20, 40 and 60 days. A significant increase in malondialdehyde and carbonyl group content, as well as decrease in catalase and increase in xanthine oxidase activity were registered under microwave exposure. Melatonin prevented the increase in malondialdehyde and carbonyl group content, and reversed the effect on catalase and xanthine oxidase activity. Both, alkaline and acid DNase activity were increased due to microwave exposure. Furthermore, microwaves caused increase in apoptosis rate (detected using Annexin V-FITC/PI kit) and reduced proliferative capacity of thymocytes (induced by ConA). However, melatonin caused decrease in alkaline and acid DNase activity, decrease in apoptotic rate and increase in proliferation rate of thymocytes. Melatonin exerts protective effects on rat thymocytes by modulating processes of apoptosis and proliferation, and causes decrease in DNA fragmentation and oxidative stress intensity under exposure to microwaves.
Gen Physiol Biophys 2013 Mar
PMID:Melatonin protects rat thymus against oxidative stress caused by exposure to microwaves and modulates proliferation/apoptosis of thymocytes. 2353 37