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J. Biol. Chem., Vol. 278, Issue 14, 12135-12143, April 4, 2003
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From the Department of Microbiology and Immunology, University of
California, San Francisco, California 94143-0414
The polyamine biosynthetic enzyme ornithine
decarboxylase (ODC) is degraded by the 26 S proteasome via a
ubiquitin-independent pathway in mammalian cells. Its degradation is
greatly accelerated by association with the polyamine-induced
regulatory protein antizyme 1 (AZ1). Mouse ODC (mODC) that is expressed
in the yeast Saccharomyces cerevisiae is also rapidly
degraded by the proteasome of that organism. We have now carried out
in vivo and in vitro studies to determine
whether S. cerevisiae proteasomes recognize mODC degradation signals. Mutations of mODC that stabilized the protein in
animal cells also did so in the fungus. Moreover, the mODC degradation
signal was able to destabilize a GFP or Ura3 reporter in GFP-mODC and
Ura3-mODC fusion proteins. Co-expression of AZ1 accelerated mODC
degradation 2-3-fold in yeast cells. The degradation of both mODC and
the endogenous yeast ODC (yODC) was unaffected in S. cerevisiae mutants with various defects in ubiquitin metabolism, and ubiquitinylated forms of mODC were not detected in yeast cells. In
addition, recombinant mODC was degraded in an ATP-dependent manner by affinity-purified yeast 26 S proteasomes in the absence of
ubiquitin. Degradation by purified yeast proteasomes was sensitive to
mutations that stabilized mODC in vivo, but was not
accelerated by recombinant AZ1. These studies demonstrate that cell
constituents required for mODC degradation are conserved between
animals and fungi, and that both mammalian and fungal ODC are subject
to proteasome-mediated proteolysis by ubiquitin-independent mechanisms.
Ubiquitin-independent Mechanisms of Mouse Ornithine Decarboxylase
Degradation Are Conserved between Mammalian and Fungal
Cells*,
,
*
This work was supported in part by Grant GM45335 from the
National Institutes of Health (to P. C.).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.
The on-line version of this article (available at
http://www.jbc.org) contains Fig. 1.
Supported by National Research Service Award Postdoctoral
Fellowship GM20527 from the National Institutes of Health.
§
To whom correspondence should be addressed: Dept. of Microbiology
and Immunology, University of California, San Francisco, CA 94143-0414. Tel.: 415-476-1783; Fax: 415-476-8201; E-mail: pcoffin@itsa.ucsf.edu.
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