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)

We have determined the nucleotide sequence of a 4.0-kilobase DNA fragment containing the genes of the PstI restriction-modification system. Two large open reading frames were identified within the sequence and were ascribed to the restriction enzyme and methylase by the analysis of a series of deletion mutants. The two genes are encoded on opposite DNA strands, and hence must be transcribed from separate promoters rather than as a polycistronic message. The sequence of the first 10 amino acids of the restriction endonuclease was determined by sequential Edman degradation of the purified protein, permitting the alignment of the polypeptide with the DNA sequence. The NH2 terminus of the modification enzyme was established by sequential Edman degradation of the protein synthesized in bacterial minicells with different radiolabeled amino acids. The initiation codons of the two genes are separated by 130 base pairs. The deduced amino acid sequences indicate that the restriction endonuclease contains 326 amino acids with a calculated Mr = 37,370; the modification enzyme is composed of 507 amino acids with a calculated Mr = 56,830. There is no significant homology between the two proteins at the level of the primary structure. Antibody raised against the purified restriction endonuclease did not immunoprecipitate the modification enzyme. The transcription initiation sites were mapped using mung bean nuclease. Both of the transcripts begin with adenosine. The initiation sites are separated by only 70 base pairs. This close proximity suggests that the promoters for the two divergent genes overlap. DNase I protection experiments show that Escherichia coli RNA polymerase has a higher affinity for the methylase promoter than for the restriction enzyme promoter.
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PMID:The organization and complete nucleotide sequence of the PstI restriction-modification system. 633 92

Escherichia coli endonuclease VI is a deoxyribonuclease specific for AP (apurinic or apyrimidinic) sites; it cleaves the phosphodiester bond immediately neighbouring the AP site on its 5' side leaving 3'-hydroxyl and 5'-phosphate ends. DNA with AP sites can be repaired in vitro with endonuclease VI, DNA polymerase I and ligase; the repair mechanism is described. E. coli has other AP endonucleases; some of them are not specific for AP sites and some of them cut 3' to the AP sites. Most of the rat liver AP endonuclease activity is in chromatin. Some is however found in other cell compartments and it has been speculated that these enzymes might be precursors of the chromatin enzyme. The chromatin AP endonuclease is specific for AP sites; it cuts 5' to the AP site. DNA with AP sites can be repaired in vitro with enzymes purified from chromatin; AP endonuclease, 5'-3 exonuclease, DNA polymerase beta and ligase.
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PMID:Repair of AP sites in DNA. 681 9

A deoxyribonuclease has been purified 570-fold from the 14-day-old chick embryos. The purified enzyme requires Mg2+ or Mn2+ ions for maximum activity. The optimum pH is 9.0 in 20 mM Tris-HCl buffer. Its isoelectric point is 6.7. NaCl and N-ethylmaleimide strongly inhibit the reaction. An apparent molecular weight of 45,000 is determined by sedimentation in a glycerol density gradient. The enzyme hydrolyzes denatured DNA 50 to 100 times more rapidly than duplex DNA. RNA and synthetic polyribonucleotides are not substrate for the enzyme. DNase A catalyzes the endonucleolytic and exonucleolytic cleavages of single-stranded DNA. The enzyme produces DNA fragments having 70 to 100 nucleotides long at early time of reaction and then degrades these DNA fragments to acid-soluble materials, of which more than 70% is mononucleotides. In the exonucleolytic attack, the enzyme initiates hydrolysis of a single-stranded DNA from 5' to 3' direction. Chick embryo DNA-binding protein gives an intensive effect on the DNase A reaction by inhibiting the endonuclease activity rather than exonuclease activity under the standard assay conditions.
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PMID:Deoxyribonuclease A of chick embryo. Partial purification and characterization of the enzyme. 682 17

Deoxyribonuclease activities were examined in isoelectric focusing fractions of non-histone, chromatin-associated and nucleoplasmic proteins of isolated normal human lymphoblastoid and mouse melanoma cell nuclei using parallel procedures. A very similar series of eight DNA endonucleases, each active on calf thymus DNA and containing no exonuclease activity, were found in the chromatin proteins of both cell lines. Several differences were observed: an activity in human cells at pI 6.6 was absent from murine cells, and there was an increased activity in mouse cells at pI 4.4 and a decreased activity at pI 7.3, as compared with corresponding human cell activities. Assay of these fractions against supercoiled, circular phage PM2 DNA showed greater activity among the fractions with acidic pI valves and slightly lower activities in the murine cells than in the human cells. Analysis of the nucleoplasmic fractions showed a series of DNA endonuclease and exonuclease activities which were again very similar between the two cell lines, although greater endonuclease activity at pI 4.4 occurred in mouse than in human nucleoplasm. These results demonstrate an entire series of deoxyribonuclease activities in both chromatin and nucleoplasm which are nearly identical in two very different mammalian cell lines, suggesting that many of these enzymes are ubiquitous in mammalian cell nuclei.
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PMID:Nuclear deoxyribonuclease activities in human lymphoblastoid and mouse melanoma cells. A comparative study. 715 90

The transfer of tetracycline resistance among strains of Clostridium difficile is described. Transfer occurred by a conjugation-like event that was insensitive to deoxyribonuclease, could not be mediated by donor culture filtrates or chloroform-treated donor cultures, and required cell-to-cell contact. Tetracycline-resistant progeny recovered from matings displayed a resistance phenotype identical to that of the donor in level of resistance, constitutive expression, and transmissibility. Although the original tetracycline-resistant donor contained 5 x 10(6)- and 22 x 10(6)-dalton plasmids, standard physical analyses of antibiotic-resistant transconjugants revealed no plasmid deoxyribonucleic acid molecules in common with the donor strain. Furthermore, tetracycline-susceptible derivatives of the original donor always possessed a plasmid complement identical to that of the resistant parental strain as determined by restriction endonuclease digestion analysis. The results indicate that the tetracycline resistance determinant(s) was not encoded by readily detectable plasmid deoxyribonucleic acid and may be chromosomally located.
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PMID:Transferable tetracycline resistance in Clostridium difficile. 727 Dec 79

An ATP-dependent deoxyribonuclease was isolated from lymphocyte nuclei. The enzyme preparation sediments with about 4 S through sucrose gradients and shows one stainable band after sodium dodecyl sulfate gel electrophoresis. We find three, possibly four, activities associated with the enzyme: a DNA-independent ATPase activity; an ATP-independent endonuclease; an ATP-dependent nuclease which degrades nicked DNA to acid-soluble material; and an unwinding activity producing single-stranded regions in nicked DNA.
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PMID:A lymphocyte ATP-dependent deoxyribonuclease. Isolation and properties. 730 58

Streptococcus pneumoniae R6X was lysogenized with bacteriophage 304 isolated after mitomycin induction of an ungrouped alpha-hemolytic streptococcus. Lysogenized pneumococci lost their capacity to undergo genetic transformation: transformability was restored after cells were spontaneously cured of their prophage. Both lysogens and nonlysogens produced activator substance (competence factor), and both bound deoxyribonucleic acid in a deoxyribonuclease-resistant form. However, nonlysogens retained deoxyribonucleic acid after washing, whereas lysogens did not. The latter did not liberate phage nor (unlike nonlysogens) degrade transforming deoxyribonucleic acid and contained normal levels of endonuclease.
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PMID:Inhibition of transformation in Streptococcus pneumoniae by lysogeny. 736 27

The genetic cassette encoding the DpnII restriction-modification system of Streptococcus pneumoniae gave transcription products of approximately 2.7 and 1.8 kilobases. The larger, mRNA1, covered both of the methylase genes, dpnM and dpnA, and the endonuclease gene dpnB; the smaller, mRNA2, covered only the dpnA and dpnB genes. Transcription of mRNA1 was shown to begin at the translation start site for dpnM, thereby producing an mRNA without any apparent ribosome-binding site for translation of the DpnM methylase. The promoter for mRNA1 was shown by base substitution and deletion analysis to consist of an extended -10 site, TaTGgTATAAT, with no required -35 site. A possible promoter further upstream with close matches to a -35 site and a nonextended -10 site was not used. A survey of 36 proven and putative promoters used by S. pneumoniae revealed that 61% of them contained the full -10 extension, although, other than the dpnM promoter, they matched at a -35 site, as well. It appears that, unlike those found in Escherichia coli, S. pneumoniae promoters frequently require an extended -10 site, and such a site can function naturally without a -35 site.
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PMID:An extended -10 promoter alone directs transcription of the DpnII operon of Streptococcus pneumoniae. 754 38

The PvuII restriction-modification system has been found to contain three genes which code for a DNA methyltransferase (MTase), a restriction endonuclease (ENase) and a small protein required for expression of the ENase-encoding gene. In addition, there is a small open reading frame (ORF) within and opposite to the MTase-encoding gene. The region containing this ORF is transcribed, and the ORF has an excellent Shine-Dalgarno sequence with an ATA start codon. A closely related ORF is present in the SmaI system. The 28-amino-acid (aa) predicted peptide from the PvuII ORF resembles a region of the PvuII ENase at the dimer interface. We have cloned this ORF, giving it an ATG start codon and putting it under the control of an inducible promoter: induction leads to a slight but significant decrease in restriction of bacteriophage lambda. We also have obtained the 28-aa synthetic peptide, and are exploring the possibility that it modulates ENase subunit association. While this peptide has no detectable effect on dimeric PvuII ENase, it inhibits renaturation of urea-denatured ENase in a concentration-dependent manner. The ORF may represent an additional safeguard during establishment of the PvuII restriction-modification system in a new host cell, helping to delay the appearance of active ENase dimers, while the MTase accumulates and protects the host chromosome.
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PMID:Gene pvuIIW: a possible modulator of PvuII endonuclease subunit association. 760 91

A deoxyribonuclease has been purified to electrophoretic homogeneity from young and old rat brain. The enzyme is an endonuclease, with an optimum pH 5.0. Divalent cations are not needed for the activity. The DNase showed highest activity towards Native DNA either as such or UV irradiated with little activity on denatured DNA, apurinic DNA or DNA pretreated with mitomycin C or actinomycin D. The enzyme hydrolyzes double stranded poly (dA-dT).(dA-dT) but not other homologous or heterologous synthetic polynucleotides. The enzyme does not excise pyrimidine dimers preferentially but acts at a site away from the dimer. The DNase was partially purified from nuclei also and both the nuclear and extra nuclear enzymes showed similar properties. The specific activity of brain DNase decreases markedly with age. DNase preparations from both young and old rats showed similar apparent molecular weight (62KD) and many other properties like elution profiles and the N-terminal amino acid. However the old enzyme was more susceptible to temperature and proteolytic digestion. These results are taken to indicate a possible role for this enzyme in recognizing conformational distortions in DNA and that altered molecules of this enzyme accumulate in aging brain.
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PMID:Purification and characterization of a deoxy-ribonuclease acting on native and UV irradiated DNA from young and aging rat brain. 784 85


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