The replacement histone H2A.Z is variously reported
as being linked to gene expression and preventing the
spread of heterochromatin in yeast, or concentrated
at heterochromatin in mammals. To resolve this
apparent dichotomy, affinity-purified antibodies
against the N-terminal region of H2A.Z, in both a triacetylatedandnon-
acetylatedstate, areusedin native
chromatin immmuno-precipitation experiments with
mononucleosomes from three chicken cell types. The
hyperacetylated species concentrates at the 50 end of
active genes, both tissue specific and housekeeping
but is absent from inactive genes, while the
unacetylated form is absent from both active and
inactive genes. A concentration of H2A.Z is also
found at insulators under circumstances implying a
link to barrier activity but not to enhancer blocking.
Although acetylated H2A.Z is widespread throughout
the interphase genome, at mitosis its acetylation is
erased, the unmodified form remaining. Thus,
although H2A.Z may operate as an epigenetic marker
for active genes, its N-terminal acetylation does not
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