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Regulation of histone acetylation in tetrahymena thermophila macro nuclei and micro nuclei


, : Regulation of histone acetylation in tetrahymena thermophila macro nuclei and micro nuclei. Journal of Biological Chemistry 257(5): 2591-2598

Histone acetylation in Tetrahymena macro- and micronuclei was studied utilizing a combination of electrophoretic and autoradiographic techniques. Histones H2A, H2B, H3 and H4 are acetylated to varying extents in the transcriptionally active macronucleus. There are few, if any, acetylated subspecies of these histones in the transcriptionally inert micronucleus, and micronuclei incorporate little radioactive acetate, either in vivo or in isolated nuclei. Butyrate is shown to inhibit histone deacetylation in Tetrahymena, both in vivo and in isolated nuclei. Incorporation of acetate into micronuclei is unaffected by high concentrations of this inhibitor, indicating that the extremely low levels of histone acetylation observed in micronuclei are not due to rapid deacetylation but probably result from the absence of histone acetylation. Macronuclear core histones are apparently composed of at least 2 classes of molecules distinguishable on the basis of their acetate turnover rates and that individual histone species differ in the distribution of their populations between these classes.

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Related references

Allis C.D.; Gorovsky M.A., 1981: Histone phosphorylation in macro nuclei and micro nuclei of tetrahymena thermophila. The patterns of histone phosphorylation in amitotically dividing, transcriptionally active macronuclei and in mitotically dividing, transcriptionally inert micronuclei of the ciliated protozoan T. thermophila were analyzed. The major phosphorylati...

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