title: Histone modification in early and late Drosophila embryos.
abstract: Levels of histone acetylation and phosphorylation have been contrasted in two developmental states of Drosophila melanogaster. The 0-2 h nuclei of the syncitial blastula are characterized by rapid mitoses and DNA replication, but there is very little transcription. In the 18 h embryo there is considerable transcription and the mitotic rate is much slower. It has been found that (1) histone H1 from 2h nuclei is not highly phosphorylated. This observation is not in accord with the view that H1 hyperphosphorylation is essential to mitosis, but is compatible with the hypothesis that H1 phosphorylation in Drosophila species is related to heterochromatization. (2) Histone H4 from 2 h embryos shows high levels of the diacetyl form (H4-Ac2), which is principally outside the nucleus. This accords with the hypothesis that H4-Ac2 is the form in which H4 is deposited on to newly replicated DNA and shows that H4 acetylation is linked not only to transcription. (3) Histone H3 acetylation is similar in 2h and in 18h embryos. As with H4, this acetylation probably correlates with chromatin assembly and is not transcription-related. (4) Histone H2B carries no modification in 2h or in 18h embryos, and H2A shows a single modification in 2h embryos and two in 18 h embryos. H2B modification is thus not essential either in mitosis or replication, whereas H2A modification is important in one or both processes. (5) The nucleosomal protein D2 is equally present in 2h and 18 h embryos.
mesh_terms: D000107:Acetylation; D000818:Animals; D002467:Cell Nucleus / Q000378:metabolism; D002843:Chromatin / Q000378:metabolism; D004331:Drosophila melanogaster / Q000196:embryology / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D006657:Histones / Q000378:metabolism*; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D013997:Time Factors
chemical_list: D002843:Chromatin; D006657:Histones