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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)

A 2000 base pair (bp) DNA fragment can be excised from sea urchin (S. purpuratus) histone gene repeat units with restriction endonuclease Eco R1. This DNA, which has been cloned in a bacterial plasmid, is known to encompass two of the five histone genes. The fragment has a single endonuclease Hind III cleavage site in one of the genes and a Hae III cleavage site in the other gene. We now report the nucleotide sequences of 62 bp adjacent to the Hind III site and 42 bp adjacent to the Hae III cleavage site. The results identify the cloned DNA as histone genes, show that it codes for histone proteins H2A and H3, and locate and orient H2A and H3 genes with respect to restriction endonuclease sites in the repeat unit.
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PMID:Identification and location of the histone H2A and H3 genes by sequence analysis of sea urchin (S. purpuratus) DNA cloned in E. coli. 79 48

Soluble fragments of chromatin obtained by Ca, Mg-dependent endonuclease digest of rat liver nuclei, have been separated by gel chromatography on Sepharose 4B into three zones, containing oligomers, tetramers--dimers and monomers, respectively. The content of nonhistone proteins and particularly lysine-rich histones is decreased with a transition from theoligomers to monomers. The average protein/DNA ratio of the monomers is equal to 1.36 and that of histone/DNA ratio--to 0.82. The dependence of the degree of chromatin digest by endonuclease on its protein content and conditions of isolation and incubation of nuclei is discussed. The chromatin monomer formed appears to be made up of a nucleosome and short portions of spacer DNA bound to some part of histone HI and nonhistone proteins.
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PMID:[Comparative characteristics of chromatin endonuclease fragments]. 88 64

Digesting of chromosomal DNA of interphase rat liver nuclei by Ca, Mg-dependent endonuclease in situ in the presence of chelating agents results in the appearance of the soluble DNP--up to 30% of the total DNA. In addition, 50% of the chromatin is solubilised after mild ultrasonication. In the absence of the chelating agents the degree of fragmentation is considerably increased. The process is accompanied by a loss of some histone and nonhistone chromosomal proteins; the nonhistone proteins are lost selectively. The preliminary removal of the nuclear membrane and significant part of the proteins by tritone X-100 promotes the chromatin degradation and the appearance of low molecular weight fragments. The DNA-fragments of solubilised chromatin are similar to the DNA-fragments of residual chromatin, but in the presence of the chelating agents the latter does not contain monomeric fragments.
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PMID:[Effect of the conditions of isolation and incubation of the nuclei on digestion of DNA chromatin by calcium- and magnesium-dependent endonuclease. Change in the spectrum of chromosomal proteins and possible role of DNA-protein interactions]. 102 91

Sucrose gradient analysis of total sea urchin DNA cleaved with the EcoRI and Hind III restriction endonucleases and identification of histone coding gene sequences by hybridization with histone mRNA have elucidated the basic organization of the histone gene repeat unit. These data, plus results obtained by electrophoretic analysis of purified endonuclease-cleaved sea urchin histone DNA and hybridization with cRNA transcribed from the eucaryotic segment of constructed plasmid chimeras cloned in E. coli, show that the several DNA sequences coding for individual histone proteins are intermingled in a 7 kilobase (kb) repeat unit. Cleavage of total sea urchin DNA with EcoRI produces 2.2 and 4.8 kb fragments, and which are contained in a 7 kb Hind III fragment. Cleavage with both enzymes reveals that the 2.2 kb EcoRI fragment contains a Hind III site 0.15--0.2 kb from an end. RNA.DNA hybridization between chimeric palsmic DNA and purified individual mRNAs isolated from sea urchin embryo polyribosomes has been used to assign coding sequences to either the 2.2 or 4.8 kb region of the histone DNA repeat unit. A map of the histone genes is proposed.
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PMID:The organization of sea urchin histone genes. 105 73

Rat-liver chromatin has bee fractionated into transcriptionally active and inactive regions [Gottesfeld et al. (1974) Proc. Nat. Acad. Sci. USA 71, 2193-2197] and the distribution of nuclease-resistant complexes in these fractions has been investigated. About half of the DNA of both fractions is resistant to attack by tne endonuclease DNase II. The nuclease-resistant structures of inactive chromatin are DNA-histone complexes (v-bodies) which sediment at 11-13 S. Template-active chromatin yields two peaks of nuclease-resistant nucleoprotein. These complexes sediment at 14 and 19 S, and contain DNA, RNA, histone, and nonhistone chromosomal proteins. Polyacrylamide gel electrophoresis reveals a complex pattern of chromatin proteins, suggesting that the complexes are heterogeneous in composition.
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PMID:Structure of transcriptionally active chromatin. 106 Jan 19

The DNA coding for histones from Strongylocentrotus purpuratus, purified up to 100-fold with the use of Hg+2-CS2-SO4 and actinomycin-CsC1 equilibrium density gradients, has been used to study the clustering of genes coding for different histones and the size of the repeating multigene cluster. When digested with EcoRI restriction endonuclease, the histone DNA is identified in two classes of fragments with molecular weights of 1.15 X 106 and 2.8 X 106, whereas after treatment of the DNA with HindIII restriction endonuclease, histone gene sequences can be identified only in a fragment of 3.95 X 106. Treatment of the DNA with both enzymes simultaneously shows that there is a HindIII site within the smaller EcoRI fragment. Partial digests with HindIII give fragment sizes that appear to be simple multiples of a 3.95 X 106 repeat. Individual histone mRNAs all hybridize to the 3.95 X 106 fragment but only to one or the other EcoRI fragments. The evidence strongly suggests a repeating unit of 3.95 X 106 containing the genes for most, if not all, the histonrs.
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PMID:Histone gene arrangement in the sea urchin, Strongylocentrotus purpuratus. 110 3

Cytosine methylation of developmentally regulated genes of the sea urchin Strongylocentrotus purpuratus was studied by using restriction-endonuclease digestion and Southern blotting. The single-copy bindin gene, the family of five cytoplasmic actin genes and the 400-fold-repeated set of five early histone genes were mostly unmethylated, but some sites exhibited partial methylation that varied throughout development. This shows that in echinoderms the methylation of DNA is not confined to the non-transcribed portion of the genome, as previously believed [Bird, Tagart & Smith (1979) Cell 17, 889-901], and may play a role in transcriptional regulation.
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PMID:DNA methylation pattern changes during development of a sea urchin. 159 Jul 64

To investigate the potentials of DNA methylation and H1 histone in regulating the action of DNA binding proteins, well ordered complexes were formed by slow salt gradient dialysis of mixtures of H1 histone with either methylated or nonmethylated DNA. The sites methylated in the plasmids were CCGG. Methylation of cytosine in this site protects the DNA against HpaII endonuclease but not against MspI. However, when the methylated DNA was complexed to H1, it was protected against MspI. The protection was only effective for a subset of the MspI restriction sites. The protection of DNA afforded by the combination of H1 binding and DNA methylation did not apply to EcoRI, PstI, or BamHI sites and so did not seem to be due to aggregation of the DNA by H1 histone. Gel retardation assays indicated that the affinity of H1 for methylated DNA was not detectably different from its affinity for nonmethylated DNA. Probably methylated DNA when bound to H1 is in a conformation that is resistant to MspI endonuclease. Such conformational changes induced by DNA methylation and H1 binding might affect the action of other DNA binding proteins, perhaps in chromatin as well as in H1.DNA complexes.
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PMID:The combination of DNA methylation and H1 histone binding inhibits the action of a restriction nuclease on plasmid DNA. 170 75

Estrogen administration to male Xenopus causes the cytoplasmic destabilization of the hepatic serum protein coding mRNAs, most notably, albumin, yet has little effect on mRNAs encoding intracellular proteins such as ferritin. This report describes an estrogen-inducible ribonuclease activity found in liver polysomes that degrades albumin mRNA 4 times faster in vitro than it degrades ferritin mRNA. This differential rate of degradation was observed upon incubation of polysome extract with free liver RNA, isolated liver mRNPs, or transcripts from plasmid vectors. A cleavage fragment consisting of a doublet of approximately 194 nucleotides in length was consistently observed upon digestion of transcripts for the full length or 5' half of albumin mRNA. The generation of this cleavage fragment was used as an assay to study properties of the polysome nuclease activity. The 194 doublet is produced by the action of a Mg(2+)-independent endonuclease. This distinguishes the Xenopus liver enzyme from the enzymes that degrade histone or c-myc mRNA in vitro. It is inactivated by 400 mM NaCl or heating at 90 degrees C, but not by placental ribonuclease inhibitor or N-ethylmaleimide. Finally, the polysomal nuclease activity does not degrade double-stranded RNA. We believe the estrogen-induced nuclease activity contains an enzyme(s) that may mediate hormone-regulated changes in mRNA stability in this tissue.
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PMID:Estrogen-induced ribonuclease activity in Xenopus liver. 193 72

The developmentally regulated sea urchin early histone gene repeat (SUEHGR) from Strongylocentrotus purpuratus was isolated as chromatin by nucleoprotein hybridization. This technique is a novel method to isolate specific sequences as chromatin. Because the purification scheme is based only on the gene sequence and is independent of other physical properties such as protein composition and transcriptional activity, we were able to isolate the same gene in different functional states. Gene size chromatin fragments were solubilized by restriction endonuclease digestion of cell nuclei. Using T7 gene 6 exonuclease, the 3'termini of the fragments were exposed and then hybridized in solution to a biotinylated oligonucleotide complementary to one end of the SUEHGR fragment. The hybrids were bound to an Avidin D matrix. DTT cleavage of the biotin linker yielded a chromatin fraction greater than 700 fold enriched in SUEHGR. Overall yields were between 2% and 15%. The purity of the isolated material was independently measured to be greater than 80%. The homogeneous native structure of the inactive genes was preserved as shown by electron microscopy and micrococcal nuclease digestion of the purified SUEHGR. Minor heterogeneity was observed for the purified active genes by micrococcal nuclease digestion but the main features of the active chromatin were preserved during isolation. This isolation offers the first opportunity to study the structure of an RNA polymerase II gene at different stages of the cell cycle and development.
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PMID:Nucleoprotein hybridization: a method for isolating active and inactive genes as chromatin. 203 Sep 47


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