## Abstract In spermiogenic nuclei of the cephalopod mollusc __Sepia officinalis__ histones are replaced by a precursorโprotamine molecule, which is later converted into protamine. Simultaneously, spermiogenic chromatin undergoes a complex structural change. Somaticโlike chromatin belonging to the
Effects of histone acetylation on chromatin structure
โ Scribed by Paola Gavazzo; Laura Vergani; Gian Carlo Mascetti; Claudio Nicolini
- Publisher
- John Wiley and Sons
- Year
- 1997
- Tongue
- English
- Weight
- 106 KB
- Volume
- 64
- Category
- Article
- ISSN
- 0730-2312
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โฆ Synopsis
The effect of histone acetylation was monitored on CHO chromatin structure, following the addition of 7 mM Na-butyrate to the cell culture medium. The properties of both control and hyperacetylated chromatins and nuclei were investigated by circular dichroism, ethidium bromide intercalation, differential scanning calorimetry, and affinity chromatography. Our results are compatible with modest but significant alterations in the various levels of chromatin organization, as a result of the charge neutralization of some lysine residues within the N-terminal region of the histonic octamer. Namely, large statistically significant differences do exist in the heat capacity thermograms of native nuclei, where unfolding into single nucleofilament of the highly packed native chromatin superfiber appears associated with acetylation; at the same time CD, EB, and affinity chromatography point to modest but consistent differences in the compactness of isolated nucleosomes and polynucleosomes.
๐ SIMILAR VOLUMES
Chromatin contains DNA, the transcriptional machinery, and structural proteins such as histones. All these components together are necessary for the physiologic control of transcription. A consideration of recent advances leads to a packaging principle for gene regulation. This packaging principle s
## Abstract In quiescent human fibroblasts stimulated to proliferate by fresh medium plus 15% serum, no changes were seen in the incorporation of ^3^Hโtryptophan into the protein of nuclear ribonucleoprotein during the first three hours following reโfeeding. This was in contrast to nonโhistone chro