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Histone variants and histone modifications in chromatin fractions from hetero chromatin rich peromyscus eremicus cells



Histone variants and histone modifications in chromatin fractions from hetero chromatin rich peromyscus eremicus cells



Experimental Cell Research 138(2): 271-286



The relationship between condensed heterochromatin and histone modification by acetylation, phosphorylation and amino acid variation was investigated. Chromatin from cultured P. eremicus cells, containing 35% constitutive heterochromatin, was fractionated into heterochromatin-enriched and 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. Sodium butyrate did inhibit deacetylation activity in the fractions, allowing histone acetylation measurements to be made. 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.

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