Abstract：
:The repressible Saccharomyces cerevisiae acid phosphatase (APase) coded by the PHO5 gene is a cell wall protein that follows the yeast secretory pathway. We had previously described the in vivo fate of a multicopy plasmid-encoded modified protein, lacking 15 out of 17 signal peptide amino acids. This modified protein accumulates mainly within the cell as an inactive unglycosylated form. However 30% of this precursor is translocated, glycosylated and dispatched to the cell wall. We establish, in the present report, that this phenomenon did not result from an overproduction of the plasmid encoded protein, since it was also observed in a normal single copy situation. The secretion persisted after a deletion including the single hydrophobic segment present in the N-terminus of the mature protein. The entry of both wild type and mutant APase into the ER was inhibited in sec62 mutants suggesting that the SEC62 gene product would not be implicated in signal peptide recognition.
journal_name
Biochimiejournal_title
Biochimieauthors
Silve S,Volland C,Hinnen A,Haguenauer-Tsapis Rdoi
10.1016/0300-9084(90)90135-4subject
Has Abstractpub_date
1990-02-01 00:00:00pages
103-14issue
2-3eissn
0300-9084issn
1638-6183pii
0300-9084(90)90135-4journal_volume
72pub_type
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