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Vol. 10, Issue 8, 2583-2594, August 1999
and
Departments of Attachment of ubiquitin to cellular proteins frequently targets
them to the 26S proteasome for degradation. In addition, ubiquitination of cell surface proteins stimulates their endocytosis and eventual degradation in the vacuole or lysosome. In the yeast
Saccharomyces cerevisiae, ubiquitin is a long-lived
protein, so it must be efficiently recycled from the proteolytic
intermediates to which it becomes linked. We identified previously a
yeast deubiquitinating enzyme, Doa4, that plays a central role in
ubiquitin-dependent proteolysis by the proteasome. Biochemical and
genetic data suggest that Doa4 action is closely linked to that of the
proteasome. Here we provide evidence that Doa4 is required for
recycling ubiquitin from ubiquitinated substrates targeted to the
proteasome and, surprisingly, to the vacuole as well. In the
doa4Biochemistry and Molecular Biology and
*Molecular Genetics and Cell Biology, University of Chicago, Chicago,
Illinois 60637
mutant, ubiquitin is strongly depleted under
certain conditions, most notably as cells approach stationary phase.
Ubiquitin depletion precedes a striking loss of cell viability in
stationary phase doa4 cells. This loss of viability
and several other defects of doa4 cells are rescued
by provision of additional ubiquitin. Ubiquitin becomes depleted in the
mutant because it is degraded much more rapidly than in wild-type
cells. Aberrant ubiquitin degradation can be partially suppressed by
mutation of the proteasome or by inactivation of vacuolar proteolysis
or endocytosis. We propose that Doa4 helps recycle ubiquitin from both
proteasome-bound ubiquitinated intermediates and membrane proteins
destined for destruction in the vacuole.
Corresponding author. E-mail
address: hoc1{at}midway.uchicago.edu.
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