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Type: Journal article
Title: Regions of variant histone His2AvD required for Drosophila development
Author: Clarkson, M.
Wells, J.
Gibson, F.
Saint, R.
Tremethick, D.
Citation: Nature, 1999; 399(6737):694-697
Issue Date: 1999
ISSN: 0028-0836
Abstract: One way in which a distinct chromosomal domain could be established to carry out a specialized function is by the localized incorporation of specific histone variants into nucleosomes. H2AZ, one such variant of the histone protein H2A, is required for the survival of Drosophila melanogaster, Tetrahymena thermophila and mice (R. Faast et al., in preparation). To search for the unique features of Drosophila H2AZ (His2AvD, also referred to as H2AvD) that are required for its essential function, we have performed amino-acid swap experiments in which residues unique to Drosophila His2AvD were replaced with equivalently positioned Drosophila H2A.1 residues. Mutated His2AvD genes encoding modified versions of this histone were transformed into Drosophila and tested for their ability to rescue null-mutant lethality. We show that the unique feature of His2AvD does not reside in its histone fold but in its carboxy-terminal domain. This C-terminal region maps to a short alpha-helix in H2A that is buried deep inside the nucleosome core.
Keywords: Nucleosomes; Animals; Xenopus; Drosophila melanogaster; Histones; Amino Acid Substitution; Mutagenesis, Site-Directed; Temperature; Binding Sites; Amino Acid Sequence; Transgenes; Models, Molecular; Molecular Sequence Data
RMID: 0030004368
DOI: 10.1038/21436
Appears in Collections:Biochemistry publications

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