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(Received for publication, August 17, 1994; and in revised form, October 18, 1994) We have cloned a Schizosaccharomyces pombe gene, here
designated cnx1, encoding the homologue of the endoplasmic
reticulum molecular chaperone calnexin. Disruption of the cnx1 gene was lethal, demonstrating that it has an essential cellular
function. Transcription of cnx1 mRNA is initiated at multiple
sites, and it can be induced by various stress treatments that lead to
the accumulation of unfolded and/or misfolded proteins in the
endoplasmic reticulum. The encoded Cnx1p protein more closely resembles
its plant and animal calnexin homologues than that of Saccharomyces
cerevisiae. Cnx1p is acidic and migrates aberrantly on
SDS-polyacrylamide gel electrophoresis, similar to its mammalian
counterparts. Cnx1p contains the hallmark KPEDWD motifs that are found
in all members of the calnexin/calreticulin family of proteins. Using
an in vitro translation-processing system, we have shown that
Cnx1p has the characteristic type I topology of calnexin proteins.
Unlike its higher eukaryotic homologues, Cnx1p has a site for N-glycosylation that was modified in an in vitro translation-processing assay.
Volume 270,
Number 9,
Issue of March 3, 1995 pp. 4845-4853
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
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