Histone variants and histone modifications in chromatin fractions from heterochromatin-rich Peromyscus cells
In order to investigate the relationship between condensed heterochromatin and histone modification by acetylation, phosphorylation and amino acid variation, chromatin from cultured Peromyscus eremicus cells, containing 35% constitutive heterochromatin, was fractionated into heterochromatin-enriched and heterochromatin-depleted fractions. The constitutive heterochromatin content of these fractions was determined from satellite DNA content. The distribution of phosphorylated and acetylated histones and amino acid variants of histone H2A in these chromatin fractions was examined by gel electrophoresis. Fractionation of histones demonstrated that endogenous histone phosphatase activity was high in chromatin fractions and could not be inhibited sufficiently to allow accurate histone phosphorylation measurements. However, sodium butyrate did inhibit deacetylation activity in the fractions, allowing histone acetylation measurements to be made. It was found that the constitutive heterochromatin content of these fractions was proportional to both their unacetylated H4 content and their more-hydrophobic H2A content. These observations support, by direct measurement, earlier experiments suggesting that constitutive heterochromatin is enriched in unacetylated arginine-rich histones, and in the more hydrophobic variant of histone H2A.
- Research Organization:
- Los Alamos National Lab., NM
- OSTI ID:
- 5987553
- Journal Information:
- Exp. Cell Res.; (United States), Vol. 138:2
- Country of Publication:
- United States
- Language:
- English
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Histone modifications and their relationship to constitutive heterochromatin content in cultured peromyscus cells
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Related Subjects
HETEROCHROMATIN
BIOCHEMISTRY
HISTONES
ACETYLATION
AMINO ACIDS
ANIMAL CELLS
CELL CULTURES
DNA
ELECTROPHORESIS
FRACTIONATION
PHOSPHORYLATION
VARIATIONS
ACYLATION
CARBOXYLIC ACIDS
CHEMICAL REACTIONS
CHEMISTRY
CHROMATIN
NUCLEIC ACIDS
ORGANIC ACIDS
ORGANIC COMPOUNDS
PROTEINS
SEPARATION PROCESSES
550200* - Biochemistry