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J. Biol. Chem., Vol. 276, Issue 28, 26656-26665, July 13, 2001
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From the Proper chromosome condensation
requires the phosphorylation of histone and nonhistone chromatin
proteins. We have used an in vitro chromosome assembly
system based on Xenopus egg cytoplasmic extracts to study
mitotic histone H3 phosphorylation. We identified a histone H3
Ser10 kinase activity associated with isolated
mitotic chromosomes. The histone H3 kinase was not affected by
inhibitors of cyclin-dependent kinases,
DNA-dependent protein kinase, p90rsk, or
cAMP-dependent protein kinase. The activity could be
selectively eluted from mitotic chromosomes and immunoprecipitated by
specific anti-X aurora-B/AIRK2 antibodies. This activity was regulated by phosphorylation. Treatment of X aurora-B immunoprecipitates with
recombinant protein phosphatase 1 (PP1) inhibited kinase activity. The
presence of PP1 on chromatin suggested that PP1 might directly regulate
the X aurora-B associated kinase activity. Indeed, incubation of
isolated interphase chromatin with the PP1-specific inhibitor I2 and
ATP generated an H3 kinase activity that was also specifically
immunoprecipitated by anti-X aurora-B antibodies. Nonetheless, we found
that stimulation of histone H3 phosphorylation in interphase cytosol
does not drive chromosome condensation or targeting of 13 S condensin
to chromatin. In summary, the chromosome-associated mitotic histone H3
Ser10 kinase is associated with X aurora-B and is inhibited
directly in interphase chromatin by PP1.
Chromatin-associated Protein Phosphatase 1 Regulates Aurora-B and
Histone H3 Phosphorylation*
,,**
School of Life Sciences, Division of
Molecular Cell Biology, University of Dundee, MSI/WTB Complex, Dow
Street, Dundee DD1 5EH, Scotland, the § Wellcome Institute
for Cell Biology, Institute of Cell and Molecular Biology, University
of Edinburgh, Swann Building, Mayfield Road, Edinburgh EH9 3JR,
Scotland, and the ¶ University of Virginia,
Charlottesville, Virginia 22908
*
This work was supported in part by Damon Runyon-Walter
Winchell Cancer Research Fund Grant DRG-1336 (to J. R. S.)
and by funds from The Wellcome Trust (05433) and the Cancer Research
Campaign (to J. R. S.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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