Effects of H1 histone and phosphorylated H1 histone on template activity and nuclease sensitivity of chromatin
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چکیده
منابع مشابه
Distribution of H1 histone in chromatin digested by micrococcal nuclease.
The relative amount of H1 histone associated with isolated nucleosomes from calf thymus was determined as a function of the extent of DNA digestion by micrococcal nuclease. Generally the amount of H1 histone associated with mononucleosomes decreases with increasing digestion until 60% of the original H1 remains associated with DNA 150 base pirs or less in size. Coincidentally, H1 histone increa...
متن کاملBinding of phosphorylated histone H1 to DNA.
A chromatin associated protein kinase was used to add 3 moles of phosphate to seryl side chains of 1 mole of histone H1. The DNA binding properties of this in vitro phosphorylated H1 were compared with those of unmodified H1. Considerably more radioactive superhelical DNA was retained on nitrocellulose filters at 20mM-40mM NaCl by phosphorylated H1 than by unmodified H1. However, zone velocity ...
متن کاملCore histone charge and linker histone H1 effects on the chromatin structure of Schizosaccharomyces pombe.
Histones are highly conserved proteins among eukaryotes. However, yeast histones are more divergent in their sequences. In particular, the histone tail regions of the fission yeast, Schizosaccharomyces pombe, have fewer lysine residues, making their charges less positive than those of higher eukaryotes. In addition, the S. pombe chromatin lacks linker histones. How these factors affected yeast ...
متن کاملHistone H1 gets Pin’d onto chromatin
Histone H1 gets Pin'd onto chromatin T he proline isomerase Pin1 limits chromosome decon-densation by stabilizing a histone's association with chromatin, Raghuram et al. reveal. Histone H1 incorporates into nucleosomes to enhance chromatin folding and condensation. Phosphory-lation by the cyclin-dependent kinase Cdk2 promotes H1's dissociation from chromatin, perhaps by altering the conformatio...
متن کاملEffects of cell cycle dependent histone H1 phosphorylation on chromatin structure and chromatin replication.
We have reconstituted salt-treated SV40 minichromosomes with differentially phosphorylated forms of histone H1 extracted from either G0-, S- or M-phase cells. Sedimentation studies revealed a clear difference between minichromosomes reconstituted with S-phase histone H1 compared with histone H1 from G0- or M-phase cells, indicating that the phosphorylation state of histone H1 has a direct effec...
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ژورنال
عنوان ژورنال: Okayama Igakkai Zasshi (Journal of Okayama Medical Association)
سال: 1982
ISSN: 0030-1558,1882-4528
DOI: 10.4044/joma1947.94.7-8_735