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Results: 81 to 84 of 84

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DNA associated with hyperacetylated histone is preferentially digested by DNase I.
Sealy L, Chalkley R
(1978) Nucleic Acids Res 5: 1863-76
MeSH Terms: Acetylation, Butyrates, Cell Line, DNA, Deoxyribonucleases, Histones, Kinetics, Protein Binding
Show Abstract · Added March 5, 2014
Butyrate-treated cells give rise to massive hyperacetylation of histones and have been used to test the idea that regions of DNA in association with hyperacetylated histones are preferentially solubilized upon digestion with DNase I. Such hyperacetylated histones can be derived from both pre-existing histones or from histone newly synthesized in the presence of butyrate which leads to extreme modification. The DNA in association with both types of hypermodified histone is equally and selectively digested.
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8 MeSH Terms
The effect of sodium butyrate on histone modification.
Sealy L, Chalkley R
(1978) Cell 14: 115-21
MeSH Terms: Acetates, Acetyl Coenzyme A, Acetylation, Amidohydrolases, Butyrates, Cell Line, Cycloheximide, Histone Deacetylase Inhibitors, Histones, Propionates
Show Abstract · Added March 5, 2014
The hyperacetylation of histones due to treatment of cultured cells with sodium butyrate has been studied. The hyperacetylation is due to inhibition of histone deacetylase. Other short chain fatty acids including acetic, isobutyric and propionic acid also produce increased modification. Histone H4 already deposited on the chromosome can be rapidly acetylated to the extent of about 70%. That 80% of histone H4 is acetylated after a 24 hr exposure to butyrate is due to the fact that incoming H4 histone is 100% acetylated and does not return to the parental unmodified form in the presence of butyrate.
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10 MeSH Terms
Cellular protein synthesis and inhibition of cell division are independent of butyrate-induced histone hyperacetylation.
Rubenstein P, Sealy L, Marshall S, Chalkley R
(1979) Nature 280: 692-3
MeSH Terms: Acetylation, Animals, Butyrates, Cell Division, Cell Line, DNA Replication, Dose-Response Relationship, Drug, Histones, Mice, Protein Biosynthesis
Added March 5, 2014
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10 MeSH Terms
Comparative studies on highly metabolically active histone acetylation.
Moore M, Jackson V, Sealy L, Chalkley R
(1979) Biochim Biophys Acta 561: 248-60
MeSH Terms: Acetylation, Animals, Cell Cycle, Cell Division, Cell Line, Dactinomycin, Histone Deacetylases, Histones, Liver Neoplasms, Experimental, Mitosis, Neoplasm Proteins, Skin, Tetrahymena pyriformis, Thymus Gland
Show Abstract · Added March 5, 2014
Histone acetate is hydrolyzed rapidly in logarithmically dividing hepatoma tissue culture cells (Jackson, V., Shires, A., Chalkley, R. and Granner, D.K. (1975) J. Biol. Chem. 250, 4856--4863). The phenomenon has been analyzed further in hepatoma tissue culture cells at various stages of the cell cycle, in stationary phase, and in the presence of actinomycin D. We also investigated the phenomenon in Tetrahymena pyriformis macronuclei, bovine thymocytes, and human foreskin fibroblasts. The data suggest that this highly metabolically active histone acetylation while altered in mitotic cells, is independent of the overall rate of cell division, and is only slightly sensitive to actinomycin D. Finally, we conclude that the same general phenomenon is found in both cancerous and normal cells and is apparently common to cells from various stages of the evolutionary scale.
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14 MeSH Terms