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Volume 272, Number 29, Issue of July 18, 1997 pp. 18051-18059
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Binding of Activated Cyclosome to p13^suc1
USE FOR AFFINITY PURIFICATION

(Received for publication, March 4, 1997)

From the Unit of Biochemistry, the B. Rappaport Faculty of Medicine and the Rappaport Institute for Research in the Medical Sciences, Technion-Israel Institute of Technology, Haifa 31096, Israel and the ^§ Institute for Cancer Research, Fox Chase Cancer Center, Philadelphia, Pennsylvania 19111

Previous studies have indicated that a ~1,500-kDa complex, designated the cyclosome or anaphase-promoting complex, has a regulated cyclin-ubiquitin ligase activity that targets cyclin B for degradation at the end of mitosis. The cyclosome is inactive in the interphase of the embryonic cell cycle and is converted to the active form in late mitosis in a phosphorylation-dependent process initiated by protein kinase Cdc2-cyclin B. We show here that the active, phosphorylated form of the cyclosome from clam oocytes binds to p13^suc1, a protein known to associate with Cdc2. The following evidence indicates that the binding of the cyclosome to p13^suc1 is not mediated via the Cdc2-cyclin B complex: (a) activated cyclosome binds to p13^suc1-Sepharose following its separation from Cdc2-cyclin B by gel filtration chromatography; (b) cyclosome from interphase extracts, activated by a kinase in which cyclin B has been replaced by an N-terminally truncated derivative fused to glutathione S-transferase, binds well to p13^suc1-Sepharose but not to glutathione-agarose. An alternative possibility, that the phosphorylated cyclosome binds directly to a phosphate-binding site of p13^suc1, is supported by the observation that the cyclosome is efficiently eluted from p13^suc1-Sepharose by phosphate-containing compounds. This information was utilized to develop a procedure for the affinity purification of the cyclosome. A factor abundant in the fraction not adsorbed to p13^suc1-Sepharose stimulates the activity of purified cyclosome. It is suggested that binding of Suc1 may have a role in the regulation of cyclosome activity.

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