Nucleic Acids Research, Vol 24, Issue 10 1816-1821, Copyright © 1996 by Oxford University Press
A Bruhat and JP Jost
We have previously shown that in vivo estradiol-dependent dephosphorylation
of MDBP-2-H1 (a member of the histone H1 family) correlates with the loss
of in vitro preferential binding to methylated DNA. To study the effects of
the phosphorylation/dephosphorylation of MDBP-2-H1 on the expression of the
avian vitellogenin II gene, we optimised an in vitro transcription system
using HeLa nuclear extracts. We show that in the absence of the
phosphorylated form of MDBP-2-H1 from rooster, methylation of the
vitellogenin II promoter does not affect the transcription. Addition of
purified MDBP-2-H1 from rooster to the in vitro transcription system
inhibits transcription more efficiently from a methylated than an
unmethylated DNA template. Dephosphorylation of rooster MDBP-2-H1 by
phosphatase treatment or estradiol treatment of rooster lead to the loss of
inhibitory activity of the protein when added to the in vitro transcription
assays. These findings indicate that the phosphorylation of MDBP-2-H1 is
essential for the repression of the transcription. Taken together these
results establish the relationship between the dephosphorylation of
MDBP-2-H1 caused by estradiol, the down regulation of its binding activity
to methylated DNA and the derepression of vitellogenin II transcription.
ARTICLES
Phosphorylation/dephosphorylation of the repressor MDBP-2-H1 selectively affects the level of transcription from a methylated promoter in vitro
Friedrich Miescher Institute, Basel, Switzerland.
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