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Volume 272, Number 15, Issue of April 11, 1997 pp. 10080-10086
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

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The Human -Type Proteasomal Subunit HsC8 Forms a Double Ringlike Structure, but Does Not Assemble into Proteasome-like Particles with the -Type Subunits HsDelta or HsBPROS26

(Received for publication, December 3, 1996, and in revised form, January 14, 1997)

Will L. H. Gerards , Jacqueline Enzlin , Markus Häner , Ine L. A. M. Hendriks , Ueli Aebi , Hans Bloemendal and Wilbert Boelens

From the Department of Biochemistry, University of Nijmegen, 6500 HB Nijmegen, The Netherlands and  Maurice E. Müller-Institut für Mikroskopische Strukturbiologie, Biozentrum der Universität Basel, CH-4056 Basel, Switzerland

The eukaryotic proteasome is a barrel-shaped protease complex made up of four seven-membered rings of which the outer and inner rings may contain up to seven different - and -type subunits, respectively. The assembly of the eukaryotic proteasome is not well understood. We cloned the cDNA for HsC8, which is one of the seven known human -type subunits, and produced the protein in Escherichia coli. Recombinant HsC8 protein forms a complex of about 540 kDa consisting of double ringlike structures, each ring containing seven subunits. Such a structure has not earlier been reported for any eukaryotic proteasome subunit, but is similar to the complex formed by the recombinant -subunit of the archaebacterium Thermoplasma acidophilum (Zwickl, P., Kleinz, J., and Baumeister, W. (1994) Nat. Struct. Biol. 1, 765-770). The ability of HsC8 to form -rings suggests that these complexes may play an important role in the initiation of proteasome assembly in eukaryotes. To test this, we used two human -type subunits, HsBPROS26 and HsDelta. Both these -type subunits, either in the proprotein or in the mature form, exist in monomers up to tetramers. In contrast to the - and -subunit of T. acidophilum, coexpression of the human -type subunits with HsC8 does not result in the formation of proteasome-like particles, which would be in agreement with the notion that proteasome assembly in eukaryotes is much more complex than in archaebacteria.

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