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J Biol Chem, Vol. 275, Issue 2, 875-882, January 14, 2000
From the Department of Biochemistry, University of Utah School of
Medicine, Salt Lake City, Utah 84132
The 19 S regulatory complex (RC) of the 26 S
proteasome is composed of at least 18 different subunits, including six
ATPases that form specific pairs S4-S7, S6-S8, and S6'-S10b in
vitro. One of the largest regulatory complex subunits, S2, was
translated in reticulocyte lysate containing
[35S]methionine and used to probe membranes containing
SDS-polyacrylamide gel electrophoresis separated RC subunits. S2 bound
to two ATPases, S4 and S7. Association of S2 with regulatory complex
subunits was also assayed by co-translation and sedimentation. S2
formed an immunoprecipitable heterotrimer upon co-translation with S4 and S7. The non-ATPase S5b also formed a ternary complex with S4 and S7
and the three proteins assembled into a tetramer with S2. Neither S2
nor S5b formed complexes with S6'-S10b dimers or with S6-S8 oligomers.
The use of chimeric ATPases demonstrated that S2 binds the
NH2-terminal region of S4 and the COOH-terminal two-thirds
of S7. Conversely, S5b binds the COOH-terminal two-thirds of S4 and to
S7's NH2-terminal region. The demonstrated association of
S2 with ATPases in the mammalian 19 S regulatory complex is consistent
with and extends the recent finding that the yeast RC is composed of
two subcomplexes, the lid and the base (Glickman, M. H., Rubin,
D. M., Coux, O., Wefes, I., Pfeifer, G., Cejka, Z., Baumeister,
W., Fried, V. A., and Finley, D. (1998) Cell 94, 615-623).
Mapping Subunit Contacts in the Regulatory Complex of the 26 S
Proteasome
S2 AND S5b FORM A TETRAMER WITH ATPase SUBUNITS S4 and S7*
,§, and
*
This work was supported by National Institutes of Health
Grant GM37009 and by a grant from the Lucille P. Markey Charitable Trust.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
These authors contributed equally to the work presented.
§
Supported by grants from the North Atlantic Treaty Organization,
the French Ministère de l'Enseignement Supérieur et de la
Recherche, and the Institut National de la Recherche Agronomique. Present address: INRA de Theix et CRNH d'Auvergne, Unité
d'Etudes du Metabolisme Azoté, 63122 Ceyrat, France.
¶
To whom correspondence should be addressed: Dept. of
Biochemistry, University of Utah School of Medicine, Salt Lake City, UT
84132. Tel.: 801-585-3128; Fax: 801-581-7959; E-mail:
rechsteiner@mailman.med.utah.edu.
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