Nucleic Acids Research, 1992, Vol. 20, No. 5 1017-1022
© 1992
MOLECULAR BIOLOGY |
Histone acetylation and globin gene switching
Portsmouth Polytechnic, Biophysics Laboratories, St Michaels Building White Swan Road, Portsmouth P01 2DT, UK
*To whom correspondence should be addressed
Received December 30, 1991. Revised February 10, 1992. Accepted February 10, 1992.
An affinity-purified antibody that recognises the epitope 
-acetyl lysine has been used to fractionate chicken erythrocyte mononucleosomes obtained from 5 and 15 day embryos. The antibody bound chromatin was enriched in multiply acetylated forms of the core histones H3, H4 and H2B, but not in ubiquitinated H2A. The DNA of these modified nucleosomes was probed with genomic sequences from the embryonic ßo gene (active at 5 days) and from the adult ßA gene (active at 15 days). Both genes were found to be highly enriched in the acetylated nucleosomes fractionated from both 5 day and from 15 day erythrocytes. We conclude that globin switching Is not linked to a change In acetylation status of the genes and that a ‘poised’ gene carries histones acetylated to a similar level as a transcriptJonally active gene. Core histone acetylation Is not therefore a direct consequence of the transcriptional process and might operate at the level of the globin locus as a general enabling step for transcription.
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