Structural basis for the subunit assembly of the anaphase-promoting complex

Anne Schreiber, Florian Stengel, Ziguo Zhang, Radoslav I. Enchev, Eric H. Kong, Edward P. Morris, Carol V. Robinson, Paula C. A. da Fonseca and David Barford ()
Additional contact information
Anne Schreiber: Section of Structural Biology, Institute of Cancer Research, Chester Beatty Laboratories
Florian Stengel: University of Oxford
Ziguo Zhang: Section of Structural Biology, Institute of Cancer Research, Chester Beatty Laboratories
Radoslav I. Enchev: Section of Structural Biology, Institute of Cancer Research, Chester Beatty Laboratories
Eric H. Kong: Section of Structural Biology, Institute of Cancer Research, Chester Beatty Laboratories
Edward P. Morris: Section of Structural Biology, Institute of Cancer Research, Chester Beatty Laboratories
Carol V. Robinson: University of Oxford
Paula C. A. da Fonseca: Section of Structural Biology, Institute of Cancer Research, Chester Beatty Laboratories
David Barford: Section of Structural Biology, Institute of Cancer Research, Chester Beatty Laboratories

Nature, 2011, vol. 470, issue 7333, 227-232

Abstract: Abstract The anaphase-promoting complex or cyclosome (APC/C) is an unusually large E3 ubiquitin ligase responsible for regulating defined cell cycle transitions. Information on how its 13 constituent proteins are assembled, and how they interact with co-activators, substrates and regulatory proteins is limited. Here, we describe a recombinant expression system that allows the reconstitution of holo APC/C and its sub-complexes that, when combined with electron microscopy, mass spectrometry and docking of crystallographic and homology-derived coordinates, provides a precise definition of the organization and structure of all essential APC/C subunits, resulting in a pseudo-atomic model for 70% of the APC/C. A lattice-like appearance of the APC/C is generated by multiple repeat motifs of most APC/C subunits. Three conserved tetratricopeptide repeat (TPR) subunits (Cdc16, Cdc23 and Cdc27) share related superhelical homo-dimeric architectures that assemble to generate a quasi-symmetrical structure. Our structure explains how this TPR sub-complex, together with additional scaffolding subunits (Apc1, Apc4 and Apc5), coordinate the juxtaposition of the catalytic and substrate recognition module (Apc2, Apc11 and Apc10 (also known as Doc1)), and TPR-phosphorylation sites, relative to co-activator, regulatory proteins and substrates.

Date: 2011
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DOI: 10.1038/nature09756

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