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J. Biol. Chem., Vol. 269, Issue 44, 27171-27174, 11, 1994
K Ura, AP Wolffe and JJ Hayes
We demonstrate that acetylation of core histone tails does not
significantly impair the ability of linker histones to bind preferentially
and asymmetrically to a defined sequence mononucleosome core reconstituted
in vitro. Thus a simple inhibition mechanism cannot explain models whereby
acetylation is causal for the observed reduction in the linker histone
content in chromatin. Other models to explain this correlation are
discussed.
Core histone acetylation does not block linker histone binding to a nucleosome including a Xenopus borealis 5 S rRNA gene
Laboratory of Molecular Embryology, NICHD, National Institutes of Health, Bethesda, Maryland 20892.
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