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Vol. 12, Issue 12, 3839-3851, December 2001
and
*Departments of Pharmacology and In mitosis, the anaphase-promoting complex (APC) regulates the
onset of sister-chromatid separation and exit from mitosis by mediating
the ubiquitination and degradation of the securin protein and mitotic
cyclins. With the use of a baculoviral expression system, we have
reconstituted the ubiquitin ligase activity of human APC. In
combination with Ubc4 or UbcH10, a heterodimeric complex of APC2 and
APC11 is sufficient to catalyze the ubiquitination of human securin and
cyclin B1. However, the minimal APC2/11 ubiquitin ligase module does
not possess substrate specificity, because it also ubiquitinates the
destruction box deletion mutants of securin and cyclin B1. Both APC11
and UbcH10 bind to the C-terminal cullin homology domain of APC2,
whereas Ubc4 interacts with APC11 directly. Zn2+-binding
and mutagenesis experiments indicate that APC11 binds Zn2+
at a 1:3 M ratio. Unlike the two Zn2+ ions of the canonical
RING-finger motif, the third Zn2+ ion of APC11 is not
essential for its ligase activity. Surprisingly, with Ubc4 as the E2
enzyme, Zn2+ ions alone are sufficient to catalyze the
ubiquitination of cyclin B1. Therefore, the Zn2+ ions of
the RING finger family of ubiquitin ligases may be directly involved in catalysis.
Biochemistry, and
Howard Hughes Medical Institute, The University of Texas
Southwestern Medical Center at Dallas, Dallas, Texas 75390-9041
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