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J. Biol. Chem., Vol. 276, Issue 37, 34810-34815, September 14, 2001
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From the Manitoba Institute of Cell Biology,
Winnipeg, Manitoba R3E 0V9, Canada
In chicken immature erythrocytes, class 1 acetylated histones are rapidly tri- and tetra-acetylated and rapidly
deacetylated. Class 2 acetylated H3 and H4 are rapidly acetylated to
mono- and di-acetylated isoforms and slowly deacetylated. Our previous
studies suggested that class 1 acetylated histones were primarily
associated with transcriptionally active DNA
(
Dynamically Acetylated Histone Association with
Transcriptionally Active and Competent Genes in the Avian Adult
-Globin Gene Domain*
A-globin) but not competent DNA (
-globin).
Chromatin salt solubility (chromatin fiber oligomerization) is directly
influenced by hyperacetylation. In this study we investigated the
association of class 1 histones with A- and -globin
DNA by measuring their loss of solubility rates in 150 mM
NaCl and 3 mM MgCl2 as a function of
hyperacetylated histone deacetylation. Expressed and competent
chromatin was associated with class 1 acetylated histones. As most
active chromatin and hyperacetylated histones are associated with the
low salt-insoluble residual nuclear material containing the nuclear
matrix, we investigated whether hyperacetylated histones are bound to
the A- and -globin DNA in this fraction. In chromatin
immunoprecipitation assays, we found that the A- and
-globin coding regions are bound to hyperacetylated H3 and H4. Our
observations are consistent with a model in which nuclear
matrix-associated histone acetyltransferases and deacetylases mediate a
dynamic attachment between active and competent chromatin and the
nuclear matrix.
*
This research was supported by Canadian Institutes of Health
Research Grant MT-9186, a Canadian Institutes of Health Research senior
scientist award (to J. R. D.), and a studentship (to V. A. S.) from
the National Cancer Institute of Canada with funds from the Canadian
Cancer Society.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.
To whom correspondence should be addressed: Manitoba Institute of
Cell Biology, 675 McDermot Ave., Winnipeg, MB, R3E OV9 Canada. Tel.:
204-787-2391; Fax: 204-787-2190; E-mail: Davie@cc.umanitoba. ca.
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