Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.31.1 (micrococcal nuclease)
 2,818 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Mononucleosomes greatly enriched in non-histone proteins were prepared by limited digestion of testis nuclei with micrococcal nuclease. Five to fifteen per cent of the chromatin was solubilized and could be separated by adjustment to 0.1 M NaCl, into a soluble fraction MN1, consisting of mononucleosomes containing the four inner histones and the small basic non-histone, H6, associated with a 140-base-pair DNA fragment. H1 was notably absent in MN1. The fraction insoluble in 0.1 M NaCl (MN2) comprised a mixture of mono-, di-, tri-, and oligosomes. MN2 monosome fraction contained the four inner histones plus H1 and lacked H6 and the length of its DNA was 170 base-pairs. Previous work had shown that limited micrococcal nuclease digestion of trout testis nuclei released a great proportion of the non-histone protein, high mobility group protein T (HMG-T). It seems likely that HMG-T is the major non-histone protein located in the linker regions of a subset of nucleosomes containing the non-histone protein H6 as a major structural component. Moreover, the presence of HMG-T renders this subset of nucleosomes very sensitive to micrococcal nuclease. Hybridization experiments were performed to demonstrate that the DNA from MN1 monosomes corresponds to a subset of the trout testis genome. This DNA subset is greatly enriched in sequences that are present in cytoplasmic RNA. Chromatin subunits enriched in their content of H6 and HMG-T could also be obtained by limited digestion of trout testis chromatin with DNase II followed by precipitation with MgCl2.
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PMID:A subset of trout testis nucleosomes enriched in transcribed DNA sequences contains high mobility group proteins as major structural components. 76 85

The technique of nick translation of nuclei (Levitt, A., Axel, R., and Cedar, H. (1979) Dev. Biol. 69, 496-505) has been used in HeLa cells to label DNase I-sensitive regions. Micrococcal nuclease digestion of the nick translated nuclei was followed by a low ionic strength gel electrophoresis system which separates different types of mononucleosomes. The major label was observed in the vicinity of high mobility group protein containing mononucleosomes. However, further analysis revealed that the particle does not sediment in the position of mononucleosomes on a sucrose gradient. Two alternative explanations are discussed as the possible source of this particle. It is either a high mobility group protein containing nucleosome in some unfolded conformation or the labeled particle originates from discrete DNA fragments, wrapped around some nonhistone proteins, located in a highly DNase I-sensitive region, which is resistant to micrococcal nuclease digestion.
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PMID:Nick translation of HeLa cell nuclei as a probe for locating DNase I-sensitive nucleosomes. 623 Mar 58

Thyroid slices were incubated with or without TSH for 2 or 5 h. Nuclei were then prepared, subjected to mild digestion with micrococcal nuclease, and centrifuged at 1200 X g. The amount of DNA in 1200 X g supernatants was increased by TSH at 5 h, but not at 2 h. In parallel studies, thyroid slices were incubated with 32Pi and labeling of acid-soluble nuclear proteins was examined. TSH-dependent increases in labeling of histones H1 and H3, and of the high mobility group protein HMG 14, were observed at 2 h; however, there were no apparent changes in TSH-dependent labeling between 2 and 5 h, in nuclease-sensitive or in bulk chromatin. These results suggest that the observed TSH-dependent changes in the micrococcal nuclease-sensitivity of thyroid nuclear chromatin were not induced directly by changes in the phosphorylation of the histones or HMG 14.
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PMID:Effects of thyrotropin on thyroid chromatin. Enhanced sensitivity to micrococcal nuclease and increased nuclear protein phosphorylation. 686 Jun 68

Limited micrococcal nuclease action on trout testis nuclei yields two mononucleosome subsets, MN1 and MN2, enriched in transcribed DNA sequences. MN1 is soluble and MN2 insoluble in 0.1 M NaCl. Electrophoresis of intact MN1 and MN2 mononucleosomes in 4% polyacrylamide gels shows that each fraction is heterogeneous and four major and several minor subcomponents can be resolved. Dissociation of the protein components of these nucleosomal particles by two-dimensional electrophoresis shows that the major component of MN1 possesses stoichiometric amounts of the four inner histones and of the high mobility group protein H6, associated with DNA fragments of 140 base pairs in length. The major component of MN2 possesses equimolar amounts of the four inner histones plus 1 molecule of H1 and H6, complexed with DNA fragments of 220 base pairs in size.
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PMID:Transcriptionally active mononucleosomes from trout testis are heterogeneous in composition. 735 38