Molecular and Cellular Biology, April 2004, p. 3562-3576, Vol. 24, No. 8
0270-7306/04/$08.00+0 DOI: 10.1128/MCB.24.8.3562-3576.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.
Bianca Habermann,2 Aliona Bogdanova,1 Alain Camasses,1,
Tobias Oelschlaegel,1 Andrej Shevchenko,1 and Wolfgang Zachariae1*
Max Planck Institute of Molecular Cell Biology and Genetics,1 Scionics Computer Innovation GmbH, Dresden, Germany2
Received 22 September 2003/ Returned for modification 24 October 2003/ Accepted 25 January 2004
The anaphase-promoting complex (APC/C) is a large ubiquitin-protein ligase which controls progression through anaphase by triggering the degradation of cell cycle regulators such as securin and B-type cyclins. The APC/C is an unusually complex ligase containing at least 10 different, evolutionarily conserved components. In contrast to APC/C's role in cell cycle regulation little is known about the functions of individual subunits and how they might interact with each other. Here, we have analyzed Swm1/Apc13, a small subunit recently identified in the budding yeast complex. Database searches revealed proteins related to Swm1/Apc13 in various organisms including humans. Both the human and the fission yeast homologues are associated with APC/C subunits, and they complement the phenotype of an SWM1 deletion mutant of budding yeast. Swm1/Apc13 promotes the stable association with the APC/C of the essential subunits Cdc16 and Cdc27. Accordingly, Swm1/Apc13 is required for ubiquitin ligase activity in vitro and for the timely execution of APC/C-dependent cell cycle events in vivo.
Permanent address: Masaryk University, Faculty of Science, Department of Analytical Chemistry, CZ-611 37 Brno, Czech Republic.
Present address: Arago Laboratory and Oceanological Observatory, 66651 Banyuls-sur-Mer, France.
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