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Vol. 9, Issue 1, 209-222, January 1998
Institut für Biochemie, Universität Stuttgart,
Pfaffenwaldring 55, D-70569 Stuttgart, Germany
We have studied components of the endoplasmic reticulum (ER)
proofreading and degradation system in the yeast Saccharomyces cerevisiae. Using a der3-1 mutant defective in
the degradation of a mutated lumenal protein, carboxypeptidase yscY
(CPY*), a gene was cloned which encodes a 64-kDa protein of the ER
membrane. Der3p was found to be identical with Hrd1p, a protein
identified to be necessary for degradation of HMG-CoA reductase. Der3p
contains five putative transmembrane domains and a long hydrophilic
C-terminal tail containing a RING-H2 finger domain which is oriented to
the ER lumen. Deletion of DER3 leads to an accumulation
of CPY* inside the ER due to a complete block of its degradation. In
addition, a DER3 null mutant allele suppresses the
temperature-dependent growth phenotype of a mutant carrying the
sec61-2 allele. This is accompanied by the
stabilization of the Sec61-2 mutant protein. In contrast,
overproduction of Der3p is lethal in a sec61-2 strain at the permissive temperature of 25°C. A mutant Der3p lacking 114 amino acids of the lumenal tail including the RING-H2 finger domain is
unable to mediate degradation of CPY* and Sec61-2p. We propose that
Der3p acts prior to retrograde transport of ER membrane and lumenal
proteins to the cytoplasm where they are subject to degradation via the
ubiquitin-proteasome system. Interestingly, in ubc6-ubc7
double mutants, CPY* accumulates in the ER, indicating the necessity of
an intact cytoplasmic proteolysis machinery for retrograde transport of
CPY*. Der3p might serve as a component programming the translocon for
retrograde transport of ER proteins, or it might be involved in
recognition through its lumenal RING-H2 motif of proteins of the ER
that are destined for degradation.
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