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J. Biol. Chem., Vol. 276, Issue 16, 12764-12768, April 20, 2001
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From the Department of Biochemistry and Microbiology, University of
Victoria, Victoria, British Columbia V8W 3P6, Canada
The folding ability of chromatin fractions
containing approximately identical nucleosome numbers and the same
linker histone composition, but with different extents of core histone
acetylation, were analyzed by analytical ultracentrifugation. It was
found that the acetylated fractions consistently exhibited a relatively small but significantly lower extent of compaction than that of their
native nonacetylated counterparts. This was regardless of the extent of
the size distribution heterogeneity of the fractions analyzed.
Furthermore the acetylated chromatin fibers exhibited an enhanced
solubility in both NaCl and MgCl2, which is neither the result of a differential binding affinity of the linker histones to
chromatin nor of an alteration in the relative amounts of the histone
H1 variants.
To whom 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.
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