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Vol. 10, Issue 11, 3927-3941, November 1999
and
*Department of Cell Biology, Harvard Medical School, Boston,
Massachusetts 02115; and The ubiquitin-dependent proteolysis of mitotic cyclin B, which is
catalyzed by the anaphase-promoting complex/cyclosome (APC/C) and
ubiquitin-conjugating enzyme H10 (UbcH10), begins around the time of
the metaphase-anaphase transition and continues through G1 phase of
the next cell cycle. We have used cell-free systems from mammalian
somatic cells collected at different cell cycle stages (G0, G1, S, G2,
and M) to investigate the regulated degradation of four targets of the
mitotic destruction machinery: cyclins A and B, geminin H (an inhibitor
of S phase identified in Xenopus), and Cut2p (an
inhibitor of anaphase onset identified in fission yeast). All four are
degraded by G1 extracts but not by extracts of S phase cells.
Maintenance of destruction during G1 requires the activity of a
PP2A-like phosphatase. Destruction of each target is dependent
on the presence of an N-terminal destruction box motif, is accelerated
by additional wild-type UbcH10 and is blocked by dominant negative
UbcH10. Destruction of each is terminated by a dominant activity that
appears in nuclei near the start of S phase. Previous work indicates
that the APC/C-dependent destruction of anaphase inhibitors is
activated after chromosome alignment at the metaphase plate. In support
of this, we show that addition of dominant negative UbcH10 to G1
extracts blocks destruction of the yeast anaphase inhibitor Cut2p in
vitro, and injection of dominant negative UbcH10 blocks anaphase onset
in vivo. Finally, we report that injection of dominant negative
Ubc3/Cdc34, whose role in G1-S control is well established and has
been implicated in kinetochore function during mitosis in
yeast, dramatically interferes with congression of chromosomes to the
metaphase plate. These results demonstrate that the regulated
ubiquitination and destruction of critical mitotic proteins is highly
conserved from yeast to humans.
Department of Cell Biology,
University of Virginia, Charlottesville, Virginia 22908
Corresponding author. E-mail
address: ruderman{at}hms.harvard.edu.
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