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:3.1.30.2 (endonuclease)
18,621 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Five broad host range lipid-containing bacteriophages PRD1, PR3, PR4, PR5 and L17 isolated from different parts of the world were compared using biological and structural criteria. Virus morphology as well as genome sizes appeared to be identical. However, these viruses could be distinguished by restriction endonuclease mapping and by their structural protein patterns in SDS--gel electrophoresis. The viruses studied thus form a very close group of lipid-containing bacteriophages. We suggest PRD1 as a model organism for this group and that the group be called the PRD1 phage group.
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PMID:Comparison of the lipid-containing bacteriophages PRD1, PR3, PR4, PR5 and L17. 732 Jul 7

Hepatitis B virus DNA contains a tightly bound protein which was not removed by healing to 60 degrees C with 2% SDS, 2% mercaptoethanol. The protein was indirectly demonstrated by the extraction of the DNA-protein complex with phenol before but not after its digestion with proteinase K. The DNA-protein complex had a lower buoyant density than protease-treated or free DNA; it was bound to glass fiber filters; it migrated at a slower rate in gel electrophoresis; and it could be radiolabeled by oxidative iodination. The binding site of the protein was mapped by extraction of restriction endonuclease digests with phenol and analysis of the digests for missing DNA fragments. The protein was localized to a site near the 5' end of the complete viral DNA strand. It remained attached to this strand after heating with SDS to 90 degrees C or treatment with 0.1 N NaOH, suggesting a covalent linkage. The 5' end of neither viral DNA strand could be phosphorylated in a reaction with polynucleotide kinase, consistent with attachment of protein to the 5' ends. The incomplete DNA strand, however, which is the strand elongated by the virion DNA polymerase reaction, did not contain a detectable amount of polypeptide as did the complete strand. The reasons for the apparent block of the 5' end of the incomplete DNA strand is thus not known. The protein bound covalently to HBV DNA could be involved in the replication of the complete viral DNA strand and/or endonucleolytic generation of linear unit-length DNA pieces from replicative intermediates, although its function and origin are not yet known.
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PMID:Hepatitis B virus contains protein attached to the 5' terminus of its complete DNA strand. 743 7

Activation of a triplet of nuclear proteins (NP42-50) was observed in human Jurkat T cell line following treatment with an antibody to CD95 (Fas/Apo-1), a cell surface molecule involved in apoptotic cell death. The nuclease activity, corresponding to a triplet of proteins observed at approximately 42, 45, and 50 kDa in size, was extractable, heat-stable, and detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis containing deoxyribonucleic acids (SDS-PAGE-DNA) assay. The NP42-50 activity requires the presence of Mg2+/Ca2+ and is insensitive to inactivation by heating at 80 degrees C for 5 min. Zinc effectively inhibited the enzymatic activity of NP42-50 on SDS-PAGE-DNA and also protected Jurkat cells from the CD95-mediated apoptosis in cell cultures. The nuclease activation, however, was not a unique pathway for the CD95-mediated cell death. The apoptosis induced by arabinofuranosyl cytosine, a chemotherapeutic agent, also activated the NP42-50 nuclease activity in Jurkat cells, suggesting that a similar cascade of subsequent events in apoptosis may occur in most instances although many different signals can initiate apoptotic cell death in various cell types. The nuclease identified by this study appears to be distinguishable from DNase I or DNase II by its molecular characteristics and its enzymatic requirements. The NP42-50, with respect to the nuclease activity closely associated with apoptotic cell death, may serve as a candidate for the endonuclease(s) involved in the cleavage of DNA into fragments during apoptosis.
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PMID:A triplet of nuclease proteins (NP42-50) is activated in human Jurkat cells undergoing apoptosis. 755 79

The 2nd endonuclease (nuclease Le3) which hydrolyzes both RNA and heat denatured DNA to 5'-nucleotides was purified from the fruit bodies of Lentinus edodes to a homogeneous state by SDS PAGE. The nuclease was different from the nuclease Le1 previously characterized [H. Shimada et al. Chem. Pharm. Bull., 39, 2633-2637 (1991)] in molecular weight, optimal pH and N-terminal amino acid sequence. The N-terminal amino acid sequence of nuclease Le3 analyzed up to the 20th residue showed that 50% of the amino acid residues are identical to nuclease Le1.
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PMID:Purification and characterization of the 2nd 5'-nucleotide-forming nuclease from Lentinus edodes. 761 9

DNA endonucleases in rat liver nuclei extracts were examined by SDS-polyacrylamide gel electrophoresis followed by zymogram analysis. Four polypeptides of 120, 54, 31 and 28 kDa, which have DNA endonuclease activity, were shown to occur in the extract isolated in the presence of phenylmethanesulfonyl fluoride (PMSF), a proteinase inhibitor. Isolation without PMSF, as well as storage at -20 degrees C, or autodigestion, resulted in multiplication of active polypeptides in the extracts. Trypsin digestion led to the appearance of an active > 140 kDa polypeptide, indicating the existence of a potential endonuclease precursor in the nuclear extract.
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PMID:In vitro proteolysis of endonucleases in rat liver nuclei extracts. 766 99

We have previously shown that in developing chicken embryos and differentiating mouse myoblasts, the demethylation of 5-metCpGs occurs through the replacement of 5-methylcytosine by cytosine (Jost, J. P. (1993) Proc. Natl. Acad. Sci. U.S.A. 90, 4685-4688; Jost, J. P. & Jost, Y.C. (1994) J. Biol. Chem. 269, 10040-10043). We have now purified over 30,000-fold a 5-methylcytosine-DNA glycosylase from 12-day-old chicken embryos. The enzyme copurifies with a mismatch-specific thymine-DNA glycosylase and an apyrimidic-endonuclease. The reaction product of the highly purified 5-methylcytosine-DNA glycosylase is 5-methylcytosine. The copurified apyrimidic-endonuclease activity cleaves 3' from the apyrimidic sugar. A 52.5-kDa peptide, isolated as a single band from preparative SDS-polyacrylamide gels, has both the 5-methylcytosine-DNA glycosylase and the mismatch-specific thymine-DNA glycosylase activities. 5-Methylcytosine-DNA glycosylase has an apparent pI of 5.5-7.5 and maximal activity between pH 6.5 and 7.5. The Km for hemimethylated oligonucleotide substrate is 8 x 10(-8) M with a Vmax of 4 x 10(-11) mol/h/micrograms proteins. 5-Methylcytosine-DNA glycosylase binds equally well to methylated and non-methylated DNA. The enzyme reacts six times faster with the hemimethylated DNA than with the same bifilarly methylated DNA sequence, and single-stranded methylated DNA is not a substrate. The action of the enzyme is distributive.
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PMID:Mechanisms of DNA demethylation in chicken embryos. Purification and properties of a 5-methylcytosine-DNA glycosylase. 773 Mar 51

Restriction endonuclease analysis was used as a new method to obtain genomic DNA fingerprints in yeast. Fifteen yeast strains belonging to the genera Saccharomyces and Zygosaccharomyces were examined. Restriction fragments obtained with ApaI or KspI endonucleases were separated by SDS-PAGE and silver-stained. Analysis of the fingerprints showed that restriction enzyme digestion of genomic DNA can be successfully applied to yeast, enabling the differentiation between strains belonging to different or to the same species or genera.
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PMID:DNA fingerprinting of yeast strains by restriction enzyme analysis. 774 55

A duck parvovirus (DPV) isolated from muscovy ducks during the epizootic in France in 1989 was purified from inoculated allanto-amniotic fluids by CsCl density gradient centrifugation and characterized. Full and empty non-enveloped icosahedral viral particles were observed banding at densities of 1.39 to 1.42 and 1.38 respectively, with a diameter of 22 to 23 nm. Viral proteins were analyzed by SDS-PAGE and the estimated molecular weights of the 3 major proteins were 91, 78 and 58 kDa. The nucleic acid was shown to be a single-stranded DNA of about 5,300 bases with terminal palindromic hairpins. These results confirm the previous classification of the virus in the family Parvoviridae established by Jestin et al. [14] on morphological and serological bases. The DPV DNA was reannealed indicating that complementary DNA strands were encapsidated. A partial restriction endonuclease map was also established. This work constitutes the first biochemical and genomic description of a muscovy duck parvovirus.
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PMID:Biochemical and genomic characterization of muscovy duck parvovirus. 782 5

TrwC is required for conjugal DNA transfer of the broad host range plasmid R388. The purified protein shows in vitro DNA helicase activity. Here we report that it also has in vitro oriT-endonuclease activity. TrwC specifically nicks oriT-containing supercoiled plasmid DNA in the presence of Mg2+, and the nicked DNA can be visualized after treatment with SDS. Sequencing of the nicked DNA showed a specific interruption of the lower DNA strand on the R388 oriT sequence. Both the 5' and the 3' ends of the nick were mapped. The 5' end was not accesible to phosphorylation by T4 polynucleotyde kinase, suggesting a covalent association with TrwC. Analysis of a collection of deletions in oriT indicated that the nucleotide sequences immediately surrounding the nic site are important, but not the only essential feature, for the nicking reaction. Comparison of the R388 nic site with previously published nic DNA sequences suggests that IncF, IncN and IncW plasmids form a family of related nic sites. During the course of this work we have also demonstrated a terminal transferase activity of Sequenase Version 2.0 DNA polymerase, as yet undocumented, which could account for some discrepancies in previously mapped nic sites in other systems.
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PMID:Nicking activity of TrwC directed against the origin of transfer of the IncW plasmid R388. 785 4

The molecular characterization of 28 clinical Actinomyces pyogenes strains was attempted. SDS-PAGE protein profiles did not allow to distinguish isolates. Restriction endonuclease analysis of total DNA gave the finest differentiation between strains but the profiles were difficult to read. Ribotypes after DNA digestion by Bst EII or Sma I have a high discriminatory power and are more helpful epidemiological markers. No relationship could be demonstrated between molecular types and clinical sources.
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PMID:Molecular typing of Actinomyces pyogenes isolates. 785 44


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