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J. Biol. Chem., Vol. 255, Issue 19, 9110-9116, Oct, 1980
J Covault and R Chalkley
We have utilized sodium butyrate to inhibit histone deacetylases in order
to study the rates of histone acetylation in hepatoma tissue culture cells.
In this manner, we have been able to observe two rates of hypermodification
of acetylated core histone. By selectively radolabeling acetylated histone
fractions based upon differences in their acetate exchange rates, we have
identified the rate of histone acetate hydrolysis and the rate of
hyperacetylation in 50 mM sodium butyrate for two distinct populations of
acetylated histone. One population, comprising no more than 15% of each of
the non-H1 histones, is characterized by rapid hyperacetylation (t 1/2
congruent to 7 min for monoacetylated H4) and the rapid (t 1/2 congruent to
3 to 7 min) removal of this modification. A second population is
deacetylated with t 1/2 congruent to 30 min and is hypermodified much less
vigorously in 50 mM sodium butyrate (t 1/2 congruent 200 to 300 min for
monoacetylated H4). Unlike the rapidly metabolized group, the fraction of
total histone in this slow population varies between the four core
histones. In addition, there appears to be no interconversion of histone
between these populations.
The identification of distinct populations of acetylated histone
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