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(Received for publication, August 25, 1995, and in revised form, August 28, 1996)
From the Institut für Genetik und Mikrobiologie,
Universität München, Maria-Ward-Strasse 1a, D-80638
München, Germany
The UBC9 gene of the yeast
Saccharomyces cerevisiae is essential for cell viability
and encodes a soluble protein of the nucleus that is metabolically
stable. Products of mutant alleles selected to confer
temperature-sensitive in vivo function were found to be
extremely short-lived at the restrictive but long-lived at the
permissive condition. An extragenic suppressor mutation was isolated
which increased thermoresistance of a ubc9-1 strain. This
suppressor turned out to stabilize the mutated gene product, indicating
that the physiological activity of ubc9-1 protein is primarily
controlled by conditional proteolysis. The labile ubc9-1 protein
appears to be a substrate for ubiquitination, and its turnover was
substantially reduced by expression of a ubiquitin derivative that
interferes with formation of multi-ubiquitin chains. Stabilization
resulted also from competitive inhibition of Ubc4-related
ubiquitin-conjugating enzymes. Activity of the proteasome complex was
crucial to rapid breakdown, whereas vacuolar proteases were
dispensable. Thus, the heat-denatured ubc9-1 protein is targeted for
proteolysis by the ubiquitin-proteasome pathway and may serve as a
useful tool to further define the process by which a misfolded
polypeptide is recognized.
Volume 271, Number 42,
Issue of October 18, 1996
pp. 25790-25796
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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