Functional domains for assembly of histones H3 and H4 into the chromatin of Xenopus embryos.
Histones H3 and H4 have a well defined structural role in the nucleosome and an established role in the regulation of transcription. We have made use of a microinjection strategy using Xenopus embryos to define the minimal structural components of H3 and H4 necessary for nucleosome assembly into metazoan chromosomes in vivo. We find that both the N-terminal tail of H4, including all sites of acetylation, and the C-terminal alpha-helix of the H4 histone fold domain are dispensable for chromatin assembly. The N-terminal tail and an N-terminal alpha-helix of H3 are also dispensable for chromatin assembly. However, the remainder of the H3 and H4 histone folds are essential for incorporation of these proteins into chromatin. We suggest that elements of the histone fold domain maintain both nucleosomal integrity and have distinct functions essential for cell viability.
Laboratory of Molecular Embryology, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892-2710, USA.
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L
Freeman
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Kurumizaka
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AP
Wolffe
D000107:Acetylation; D000818:Animals; D002470:Cell Survival; D002843:Chromatin / Q000378:metabolism* / Q000648:ultrastructure; D004247:DNA / Q000737:chemistry / Q000378:metabolism; D004625:Embryo, Nonmammalian; D006657:Histones / Q000096:biosynthesis* / Q000737:chemistry*; D008961:Models, Structural; D016297:Mutagenesis, Site-Directed; D009707:Nucleosomes / Q000378:metabolism / Q000648:ultrastructure; D017354:Point Mutation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry; D014981:Xenopus
D002843:Chromatin; D006657:Histones; D009707:Nucleosomes; D011994:Recombinant Proteins; D004247:DNA