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J Biol Chem, Vol. 275, Issue 19, 14336-14345, May 12, 2000
From the Eukaryotic cells contain various types of
proteasomes. Core 20 S proteasomes (abbreviated 20 S below) have two
binding sites for the regulatory particles, PA700 and PA28. PA700-20
S-PA700 complexes are known as 26 S proteasomes and are
ATP-dependent machines that degrade cell proteins. PA28 is
found both in previously described complexes of the type PA28-20
S-PA28 and in complexes that also contain PA700, as PA700-20 S-PA28.
We refer to the latter as "hybrid proteasomes." The relative
amounts of the various types of proteasomes in HeLa extracts were
determined by a combination of immunoprecipitation and immunoblotting.
Hybrid proteasomes accounted for about a fourth of all proteasomes in
the extracts. Association of PA28 and proteasomes proved to be
ATP-dependent. Hybrid proteasomes catalyzed
ATP-dependent degradation of ornithine decarboxylase (ODC)
without ubiquitinylation, as do 26 S proteasomes. In contrast, the
homo-PA28 complex (PA28-20 S-PA28) was incapable of degrading ODC.
Intriguingly, a major immunomodulatory cytokine, interferon-
Hybrid Proteasomes
INDUCTION BY INTERFERON-
AND CONTRIBUTION TO ATP-DEPENDENT
PROTEOLYSIS*
,
,
Tokyo Metropolitan Institute of Medical
Science and Core Rsearch for Evolutional Science and Technology, Japan
Science and Technology Corporation, 3-18-22 Honkomagome, Bunkyo-ku,
Tokyo 113-8613, Japan, the § Department of Biochemistry 2, Jikei University School of Medicine, Minato-ku, Tokyo 105-8461, Japan,
the ¶ Department of Biochemistry, Oita Medical University, 1-1 Idaigaoka, Hasama-machi, Oita 879-5593, Japan, the Department of
Research, UP Science, Inc., 1, Taya-cho, Sakae-ku, Yokohama 244-8588, Japan, and the ** August Krogh Institute, University of Copenhagen, 13 Universitetsparken, DK 2100 Copenhagen, Denmark
,
appreciably enhanced the ODC degradation in HeLa and SW620 cells
through induction of the hybrid proteasome, which may also be
responsible for the immunological processing of intracellular antigens.
Taken together, we report here for the first time the existence of two
types of ATP-dependent proteases, the 26 S proteasome and
the hybrid proteasome, which appear to share the
ATP-dependent proteolytic pathway in mammalian cells.
*
This work was supported in part by Grants-in-aid for
Scientific Research on Priority Areas (Intracellular Proteolysis) from the Ministry of Education, Science, Sports, and Culture of Japan and by
grants from the Human Frontier Science Promotion Organization.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.
To whom correspondence should be addressed. Fax:
81-3-3823-2237; E-mail: tanakak@rinshoken.or.jp.
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