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J. Biol. Chem., Vol. 275, Issue 45, 35013-35020, November 10, 2000
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From the Department of Biochemistry and Microbiology, University of
Victoria, Victoria V8W 3P6, British Columbia, Canada
The nature of the structural changes induced by
histone acetylation at the different levels of chromatin organization
has been very elusive. At the histone level, it has been proposed on
several occasions that acetylation may induce an
Acetylation Increases the
-Helical Content of the Histone
Tails of the Nucleosome*
-helical conformation of their acetylated N-terminal domains (tails). In an
attempt to provide experimental support for this hypothesis, we have
purified and characterized the tail of histone H4 in its native and
mono-, di-, tri-, and tetra- acetylated form. The circular dichroism
analysis of these peptides shows conclusively that acetylation does
increase their -helical content. Furthermore, the same spectroscopic analysis shows that this is also true for both the acetylated nucleosome core particle and the whole histone octamer in solution. In
contrast to the native tails in which the -helical organization appears to be dependent upon interaction of these histone regions with
DNA, the acetylated tails show an increase in -helical content that
does not depend on such an interaction.
*
This work was supported by Medical Research Council of
Canada Grant MT-13104 (to J. A.).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 all correspondence should be addressed: Dept. of
Biochemistry and Microbiology, University of Victoria, P.O. Box 3055, Petch Bldg. 220, Victoria, British Columbia V8W 3P6, Canada. Tel.: 250-721-8863; Fax: 250-721-8855; E-mail: jausio@uvic.ca.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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