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A more recent version of this article appeared on April 1, 2002
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Submitted on October 10, 2001
Accepted on December 24, 2001
1 Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester MA 01655, USA
2 Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester MA 01655, USA (present address: Department of Developmental and Molecular Biology, Albert Einstein College of Medicine, Bronx NY 10461)
* Corresponding author. E-mail address: donald.tipper{at}umassmed.edu.
Yeast Protein Insertion Orientation (PIO) mutants were isolated by selecting for growth on sucrose in cells in which the only source of invertase is a C-terminal fusion to a transmembrane (TM) protein. Only the fraction with an exocellular C-terminus can be processed to secreted invertase and this fraction is constrained to 2-3% by a strong charge difference signal. Identified pio mutants increased this to 9-12%. PIO1 is SPF1, encoding a P-type ATPase located in the ER or Golgi. spf1-null mutants are modestly sensitive to EGTA. Sensitivity is considerably greater in an spf1 pmr1 double mutant, although PIO is not further disturbed. Pmr1p is the Golgi Ca2+ ATPase and Spf1p may be the equivalent ER pump. PIO2 is STE24, a metalloprotease anchored in the ER membrane. Like Spf1p, Ste24p is expressed in all yeast cell types and belongs to a highly conserved protein family. The effects of ste24-null and spf1-null mutations on invertase secretion are additive, cell generation time is increased 50% and cells become sensitive to cold and to heat shock. Ste24p and Rce1p cleave the C-AAX bond of farnesylated CAAX box proteins. The closest paralog of SPF1 is YOR291w. Neither rce1-null nor yor291w-null mutations affected PIO or the phenotype of spf1- or ste24-null mutants. Mutations in PIO3 (unidentified) cause a weaker Pio phenotype, enhanced by a null mutation in BMH1, one of two yeast 14-3-3 proteins.
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