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The replacement histone H2A.Z in a hyperacetylated form is a feature of active genes in the chicken

Bruce, K., Myers, F.A., Mantouvalou, E., Lefevre, P., Greaves, I., Bonifer, C., Tremethick, D.J., Thorne, A.W. and Crane-Robinson, C. (2005) The replacement histone H2A.Z in a hyperacetylated form is a feature of active genes in the chicken. Nucleic Acids Research, 33 (17). pp. 5633-5639. ISSN 1362-4962

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Abstract

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 triacetylatedandnon- acetylatedstate, areusedin native chromatin immmuno-precipitation experiments with mononucleosomes from three chicken cell types. The hyperacetylated species concentrates at the 50 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.

Item Type: Article
Copyright, Publisher and Additional Information: © 2005, the authors. Published by Oxford University Press. Supplementary material available at http://nar.oxfordjournals.org/cgi/reprint/33/17/5633
Institution: The University of Leeds
Academic Units: The University of Leeds > Faculty of Medicine and Health (Leeds) > Institute of Molecular Medicine (LIMM) (Leeds) > Section of Genetics (Leeds)
Depositing User: Repository Officer
Date Deposited: 13 Mar 2006
Last Modified: 13 Jun 2014 14:24
Published Version: http://nar.oxfordjournals.org/cgi/reprint/33/17/56...
Status: Published
Refereed: Yes
Identification Number: 10.1093/nar/gki874
URI: http://eprints.whiterose.ac.uk/id/eprint/968

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