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(Received for publication, February 21, 1996)
From the Effects of okadaic acid (OA), a protein
phosphatase inhibitor, on chromatin structure and phosphorylation of
histones were examined using HeLa and N18 cells. The chromatin
condensation in HeLa cells was mild and resemble prometaphase nuclei,
while the condensation in N18 cells was extensive and chromatin became
a compact body. H2A in HeLa cells was extensively and consistently
phosphorylated at the same site throughout the cell cycle, and H3 was
demonstrated to be phosphorylated at the mitosis-specific site
Ser10. In contrast, H1 phosphorylation was rapidly
decreased in most sites within 3 h. The reduction of H1 phosphorylation
was accompanied by a quantitative change in the set of H1
phosphopeptides. During the early phase of the OA treatment, H1
phosphorylation was transiently elevated in tandem, whereas H3
phosphorylation reached a maximum somewhat later. The results suggest
that mitosis-specific events (cdc2/H1 kinase activation, H1
superphosphorylation, mitosis-specific H3 phosphorylation and chromatin
condensation) induced by OA are sequentially associated. The changes
appear to reflect a molecular mechanism similar to that operating in
normal mitosis.
Volume 271, Number 22,
Issue of May 31, 1996
pp. 13197-13201
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
INDUCTION OF MITOSIS-SPECIFIC H3 PHOSPHORYLATION AND CHROMATIN
CONDENSATION IN MAMMALIAN INTERPHASE CELLS
,
and
Aichi Cancer Center, Research Institute,
Laboratory of Cell Biology and 
Laboratory of Ultrastructure
Research, Chikusa-ku and the ¶ Nagoya University, Faculty of
Science, Institute of Molecular Biology, Nagoya 464, Japan
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