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J Biol Chem, Vol. 274, Issue 6, 3453-3460, February 5, 1999
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From the Polypeptide import into the yeast endoplasmic
reticulum (ER) requires two hsp70s, Ssa1p in the cytosol and BiP
(Kar2p) in the ER lumen. After import, aberrant polypeptides may be
exported to the cytoplasm for degradation by the proteasome, and
defects in the ER chaperone calnexin (Cne1p) compromise their
degradation. Both import and export require BiP and the Sec61p
translocation complex, suggesting that import and export may be
mechanistically related. We now show that the cne1 Department of Biological Sciences,
University of Pittsburgh, Pittsburgh, Pennsylvania 15260 and the
¶ Department of Biology, University of Nevada,
Reno, Nevada 89557
and
two kar2 mutant alleles exhibit a synthetic interaction and
that the export and degradation of pro-
factor is defective in
kar2 mutant microsomes. Pulse-chase analysis indicates that
A1PiZ, another substrate for degradation, is stabilized in the
kar2 strains at the restrictive temperature. Because two of
the kar2 mutants examined are proficient for polypeptide import, the roles of BiP during ER protein export and import differ, indicating that these processes must be mechanistically distinct. To
examine whether Ssa1p drives polypeptides from the ER and is also
required for degradation, we assembled reactions using strains either
containing a mutation in SSA1 or in which the level of Ssa1p could be regulated. We found that pro- factor and A1PiZ were
degraded normally, indicating further that import and export are
distinct and that other cytosolic factors may pull polypeptides from
the ER.
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