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Originally published In Press as doi:10.1074/jbc.M009472200 on March 26, 2001

J. Biol. Chem., Vol. 276, Issue 23, 20197-20205, June 8, 2001
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Targeted and Extended Acetylation of Histones H4 and H3 at Active and Inactive Genes in Chicken Embryo Erythrocytes*

Fiona A. Myers, Dain R. Evans, Alison L. ClaytonDagger , Alan W. Thorne, and Colyn Crane-Robinson§

From the Biophysics Laboratories, Institute of Biomedical and Biomolecular Sciences, Faculty of Science, University of Portsmouth, Portsmouth PO1 2DT, United Kingdom

Affinity-purified polyclonal antibodies recognizing the most highly acetylated forms of histones H3 and H4 were used in immunoprecipitation assays with chromatin fragments derived from 15-day chicken embryo erythrocytes by micrococcal nuclease digestion. The distribution of hyperacetylated H4 and H3 was mapped at the housekeeping gene, glyceraldehyde 3-phosphate dehydrogenase (GAPDH), and the tissue-specific gene, carbonic anhydrase (CA). H3 and H4 acetylation was found targeted to the CpG island region at the 5' end of both these genes, falling off in the downstream direction. In contrast, at the beta A-globin gene, both H3 and H4 are highly acetylated throughout the gene and at the downstream enhancer, with a maximum at the promoter. Low level acetylation was observed at the 5' end of the inactive ovalbumin gene. Run-on assays to measure ongoing transcription showed that the GAPDH and CA genes are transcribed at a much lower rate than the adult beta A-globin gene. The extensive high level acetylation at the beta A-globin gene correlates most simply with its high rate of transcription. The targeted acetylation of histones H3 and H4 at the GAPDH and CA genes is consistent with a role in transcriptional initiation and implies that transcriptional elongation does not necessarily require hyperacetylation.

* This work was made possible by the generous support of the Wellcome Trust.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Present address: Dept. of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.

§ To whom correspondence should be addressed. Tel.: 44-23-92842055, Fax: 44-23-92842053; E-mail: colyn.crane-robinson@port.ac.uk.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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