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Nucleic Acids Research Dec 1989
Topics: Alleles; Cathepsin E; Cathepsins; Chromosomes, Human, Pair 1; Deoxyribonuclease HpaII; Deoxyribonucleases, Type II Site-Specific; Genes; Humans; Polymorphism, Restriction Fragment Length
PubMed: 2481262
DOI: 10.1093/nar/17.23.10147 -
The Journal of Antibiotics Feb 1982
Topics: Deoxyribonucleases; Micromonospora
PubMed: 7076569
DOI: 10.7164/antibiotics.35.248 -
Structure (London, England : 1993) Jun 2009In this issue of Structure, Wiedenheft et al. describe the structure and activity of Cas1, the only protein associated with all CRISPR loci. Cas1 is a metal-dependent...
In this issue of Structure, Wiedenheft et al. describe the structure and activity of Cas1, the only protein associated with all CRISPR loci. Cas1 is a metal-dependent deoxyribonuclease, consistent with a role in the adaptation phase of CRISPR immunity against invading nucleic acids.
Topics: Bacteriophages; DNA, Bacterial; Deoxyribonucleases; Immunity; Models, Immunological; Proteins; Repetitive Sequences, Nucleic Acid
PubMed: 19523896
DOI: 10.1016/j.str.2009.05.002 -
Journal of Clinical Microbiology Jan 1988Restriction endonuclease cleavage site analysis was used to differentiate between mouse adenovirus (MAV) types 1 and 2 strains. Viral DNA of suitable purity and quantity...
Restriction endonuclease cleavage site analysis was used to differentiate between mouse adenovirus (MAV) types 1 and 2 strains. Viral DNA of suitable purity and quantity for multiple enzymatic digestions was obtained from cloned CMT-93 mouse tumor cells infected with each type of MAV. Clear differences between the MAV-1 (FL) and MAV-2 (K87) genomes were observed after cleavage with restriction enzymes such as BglII, EcoRI, and PaeR7. Fast electrophoresis of DNA fragments in miniature agarose slab gels allowed rapid and unequivocal identification of the MAV strains. This relatively simple and accurate method should be quite useful to determine the different modes of transmission of mouse adenoviruses and their presence in various animal populations.
Topics: Adenoviridae; Animals; Bacterial Proteins; DNA Restriction Enzymes; DNA, Viral; Deoxyribonuclease EcoRI; Deoxyribonucleases, Type II Site-Specific; Mice
PubMed: 2830299
DOI: 10.1128/jcm.26.1.31-33.1988 -
The Journal of Biological Chemistry Feb 1970
Topics: Adenosine Triphosphate; Benzoates; Carbon Isotopes; Cell-Free System; Centrifugation, Zonal; Chemical Precipitation; Chromatography, Gel; Chromatography, Ion Exchange; DNA, Bacterial; Deoxyribonucleases; Escherichia coli; Glycols; Hydrogen-Ion Concentration; Kinetics; Magnesium; Mercury; Methods; Micrococcus; Nucleic Acid Denaturation; Organometallic Compounds; Pancreas; Phosphorus Isotopes; Quaternary Ammonium Compounds; Solubility; Streptomycin; Sulfates; Temperature; Viscosity
PubMed: 4906634
DOI: No ID Found -
Journal of Bacteriology Nov 1969A total of 20 genera of yeasts and yeastlike organisms were tested for their ability to produce an extracellular deoxyribonuclease. Results indicate that ability to...
A total of 20 genera of yeasts and yeastlike organisms were tested for their ability to produce an extracellular deoxyribonuclease. Results indicate that ability to produce the enzyme appears to be a specific characteristic of the three genera Rhodotorula, Cryptococcus, and Tremella. A single strain of Endomycopsis fibuligera was also shown to be positive for the enzyme. In comparing the ability of the organisms to excrete extracellular deoxyribonuclease with their ability to produce urease, a surprisingly close correlation was found. With the exception of Lipomyces starkeyi, all the organisms which were deoxyribonuclease-negative were also urease-negative. Of those organisms which were deoxyribonuclease-positive, only E. fibuligera was urease-negative. The ability of cryptococci to produce extracellular deoxyribonuclease is discussed in relation to the implication which this finding may have for the taxonomy and phylogeny of the genus.
Topics: Culture Media; Deoxyribonucleases; Methods; Urease; Yeasts
PubMed: 5354946
DOI: 10.1128/jb.100.2.760-762.1969 -
Journal of Biochemistry Apr 1980The acid deoxyribonucleases [DNase II; EC 3.1.4.6] in human urine were purified approximately 400- to 500-fold by phosphocellulose chromatography, gel filtration on...
The acid deoxyribonucleases [DNase II; EC 3.1.4.6] in human urine were purified approximately 400- to 500-fold by phosphocellulose chromatography, gel filtration on Sephadex G-75 and isoelectric focusing, with a total recovery of 22%. The enzymes were present in a least three forms with different isoelectric points, pHs 6.4, 6.6, and 6.8. However, other properties were essentially similar. The enzymes did not require divalent cations for activity, and the optimal pHs were at 5.1 to 5.3 in 33 mM acetate buffer. They had a molecular weight of around 36,000, as estimated by gel filtration on Sephadex G-75. The enzymes were endonucleases which hydrolyzed native, double-stranded DNA about 5 to 15 times faster than thermally denatured DNA. The products formed from native DNA were 3'-phosphoryl- and 5'-hydroxy-terminated oligonucleotides. The average chain length of the limit digests with these enzymes was approximately 11 to 15, and the major fragments were longer than pentanucleotides. The final preparations were free of nonspecific acid and alkaline phosphatases and phosphodiesterase, but contained contaminating ribonuclease activity.
Topics: Deoxyribonucleases; Drug Stability; Endodeoxyribonucleases; Endonucleases; Humans; Hydrogen-Ion Concentration; Isoelectric Focusing; Kinetics; Molecular Weight; Substrate Specificity
PubMed: 6248503
DOI: No ID Found -
The Journal of Biological Chemistry Apr 2000Caspase-activated DNase (CAD) is an enzyme that cleaves chromosomal DNA in apoptotic cells. Here, we identified a DNase in Drosophila Schneider cells that can be...
Caspase-activated DNase (CAD) is an enzyme that cleaves chromosomal DNA in apoptotic cells. Here, we identified a DNase in Drosophila Schneider cells that can be activated by caspase 3, and purified it as a complex of two subunits (p32 and p20). Using primers based on the amino acid sequence of the purified proteins, a cDNA coding for Drosophila CAD (dCAD) was cloned. The polypeptide encoded by the cDNA contained 450 amino acids with a calculated M(r) of 52,057, and showed significant homology with human and mouse CAD (22% identity). Mammalian CADs carry a nuclear localization signal at the C terminus. In contrast, dCAD lacked the corresponding sequence, and the purified dCAD did not cause DNA fragmentation in nuclei in a cell-free system. When dCAD was co-expressed in COS cells with Drosophila inhibitor of CAD (dICAD), a 52-kDa dCAD was produced as a heterotetrameric complex with dICAD. When the complex was treated with human caspase 3 or Drosophila caspase (drICE), the dICAD was cleaved, and released from dCAD. In addition, dCAD was also cleaved by these caspases, and behaved as a (p32)(2)(p20)(2) complex in gel filtration. When a Drosophila neuronal cell line was induced to apoptosis by treatment with a kinase inhibitor, both dCAD and dICAD were cleaved. These results indicated that unlike mammalian CAD, Drosophila CAD must be cleaved by caspases to be activated.
Topics: Amino Acid Sequence; Animals; Apoptosis; Base Sequence; Blotting, Western; COS Cells; Caspase 3; Caspases; Cell Line; Cell Nucleus; Chromatography, Gel; Cloning, Molecular; DNA Fragmentation; DNA, Complementary; Deoxyribonucleases; Drosophila melanogaster; Enzyme Activation; Humans; Molecular Sequence Data; Sequence Homology, Amino Acid
PubMed: 10777599
DOI: 10.1074/jbc.275.17.12978 -
The Journal of Biological Chemistry Mar 1982Endonuclease V of bacteriophage T4 has been purified to physical homogeneity from T4D-infected Escherichia coli 1100. The enzyme, whose molecular weight is 16,000,...
Endonuclease V of bacteriophage T4 has been purified to physical homogeneity from T4D-infected Escherichia coli 1100. The enzyme, whose molecular weight is 16,000, possessed two distinct catalytic activities, a pyrimidine dimer-DNA glycosylase and an apurinic/apyrimidinic endonuclease. They acted on UV-irradiated poly(dA) . poly(dT) in a sequential manner; the glycosylase cleaved the N-glycosyl bond between the 5'-pyrimidine of a dimer and the corresponding sugar and then the endonuclease hydrolyzed a phosphodiester bond on the 3'-side of the apyrimidinic site. The 5'-termini thus generated were phosphorylated by T4 polynucleotide kinase only after they had been subjected to direct photoreversal and then treated with alkaline phosphatase. By using two phage mutants, uvs-5 and uvs-13, it was shown that occurrence of an amber mutation in the denV gene caused a simultaneous loss of the two activities. Suppression of the mutation of uvs-5 rendered both activities partially active. When the mutation of uvs-13 was suppressed, a mutant form of enzyme that possessed only a glycosylase activity was produced. This suggests that there are two distinct domains in a single enzyme, each of which corresponds to one of the activities.
Topics: Deoxyribonuclease (Pyrimidine Dimer); Deoxyribonucleases; Endodeoxyribonucleases; Endonucleases; Escherichia coli; Kinetics; Molecular Weight; Mutation; Osmolar Concentration; T-Phages; Ultraviolet Rays; Viral Proteins
PubMed: 6277906
DOI: No ID Found -
Journal of Virology Jul 1984Epstein-Barr virus (EBV), isolated from P3HR-1 cells, induces early antigen and viral capsid antigen upon infection of human B-lymphoblasts. The strong early antigen-...
Epstein-Barr virus (EBV), isolated from P3HR-1 cells, induces early antigen and viral capsid antigen upon infection of human B-lymphoblasts. The strong early antigen- and viral capsid antigen-inducing activity is only observed in P3HR-1 virus preparations harboring particles with defective genomes, suggesting that this biological activity is directly associated with the defective DNA population. After infection of EBV genome-carrying Raji or EBV genome-negative BJAB cells, defective genomes of P3HR-1 EBV DNA are replicated in excess, depending on the multiplicity of infecting EBV particles. Hybridization of the DNA from such infected cells with 32P-labeled EBV DNA after HindIII cleavage reveals six hypermolar fragments. Mapping of these fragments shows that they form one defective genome unit containing four nonadjacent regions (alpha, beta, gamma, and delta) of the nondefective P3HR-1 EBV DNA. Two of the segments (alpha and beta) contain ca. 17 and 13 megadaltons, respectively, from the terminal regions of the P3HR-1 genome, whereas the two smaller segments (gamma and delta) contain ca. 3.7 and 3.0 megadaltons, respectively, originating from the central portion of the genome. In the defective molecule, the regions gamma and delta are present in the opposite orientation compared with nondefective P3HR-1 EBV DNA. Tandem concatemers are formed by fusion of the alpha and beta regions. Our model suggests that tandem concatemers of three defective genome units can be packaged into virions in P3HR-1 cells.
Topics: Base Sequence; Cell Line; DNA Restriction Enzymes; DNA, Viral; Deoxyribonuclease BamHI; Deoxyribonucleases, Type II Site-Specific; Herpesvirus 4, Human; Nucleic Acid Conformation; Nucleic Acid Hybridization
PubMed: 6328039
DOI: 10.1128/JVI.51.1.199-207.1984