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J Biol Chem, Vol. 274, Issue 20, 14500-14507, May 14, 1999
From the The anaphase-promoting complex/cyclosome (APC) is
a ubiquitin-protein ligase whose activity is essential for progression
through mitosis. The vertebrate APC is thought to be composed of 8 subunits, whereas in budding yeast several additional APC-associated
proteins have been identified, including a 33-kDa protein called Doc1
or Apc10. Here, we show that Doc1/Apc10 is a subunit of the yeast APC
throughout the cell cycle. Mutation of Doc1/Apc10 inactivates the APC
without destabilizing the complex. An ortholog of Doc1/Apc10, which we
call APC10, is associated with the APC in different vertebrates, including humans and frogs. Biochemical fractionation experiments and
mass spectrometric analysis of a component of the purified human APC
show that APC10 is a genuine APC subunit whose cellular levels or
association with the APC are not cell cycle-regulated. We have further
identified an APC10 homology region, which we propose to call the DOC
domain, in several protein sequences that also contain either cullin or
HECT domains. Cullins are present in several ubiquitination complexes
including the APC, whereas HECT domains represent the catalytic core of
a different type of ubiquitin-protein ligase. DOC domains may therefore
be important for reactions catalyzed by several types of
ubiquitin-protein ligases.
Characterization of the DOC1/APC10 Subunit of the Yeast and the
Human Anaphase-promoting Complex
,,,,,
Research Institute of Molecular Pathology,
Dr.-Bohr Gasse 7, A-1030 Vienna, Austria and § Protein
Interaction Laboratory, University of Southern Denmark, Odense
University, Campusvej 55, DK-5230 Odense M, Denmark
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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