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Vol. 14, No. 23, pp. 3003-3013, December 1, 2000
Department of Biology, The Johns Hopkins University,
Baltimore, Maryland 21218, USA
Posttranslational modifications of the N-terminal tails of the core
histones within the nucleosome particle are thought to act as signals
from the chromatin to the cell for various processes. The experiments
presented here show that the acetylation of histones H3 and H4 in
polytene chromosomes does not change during heat shock. In contrast,
the global level of phosphorylated H3 decreased dramatically during a
heat shock, with an observed increase in H3 phosphorylation at the heat
shock loci. Additional experiments confirm that this change in
phosphorylated H3 distribution is dependent on functional heat shock
transcription factor activity. These experiments suggest that H3
phosphorylation has an important role in the induction of transcription
during the heat shock response.
[Key Words: Histone phosphorylation; histone acetylation; transcription; heat shock, chromatin]
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