Published online 4 October 2005
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The replacement histone H2A.Z in a hyperacetylated form is a feature of active genes in the chicken
Biophysics Laboratories, Institute of Biomedical and Biomolecular Sciences, Faculty of Science, University of Portsmouth Portsmouth, PO1 2DT, UK 1Molecular Medicine Unit, St James's University Hospital, University of Leeds Leeds, LS9 7TF, UK 2The John Curtin School of Medical Research, The Australian National University PO Box 334, Canberra, Australian Capital Territory 2601
*To whom correspondence should be addressed. Tel: +44 2392842055; Fax: +44 2392842053; Email: colyn.crane-robinson{at}port.ac.uk
Received June 6, 2005. Revised August 23, 2005. Accepted September 13, 2005.
The replacement histone H2A.Z is variously reported as being linked to gene expression and preventing the spread of heterochromatin in yeast, or concentrated at heterochromatin in mammals. To resolve this apparent dichotomy, affinity-purified antibodies against the N-terminal region of H2A.Z, in both a triacetylated and non-acetylated state, are used in native chromatin immmuno-precipitation experiments with mononucleosomes from three chicken cell types. The hyperacetylated species concentrates at the 5' end of active genes, both tissue specific and housekeeping but is absent from inactive genes, while the unacetylated form is absent from both active and inactive genes. A concentration of H2A.Z is also found at insulators under circumstances implying a link to barrier activity but not to enhancer blocking. Although acetylated H2A.Z is widespread throughout the interphase genome, at mitosis its acetylation is erased, the unmodified form remaining. Thus, although H2A.Z may operate as an epigenetic marker for active genes, its N-terminal acetylation does not.
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