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The calnexin-independent state does not compensate for all calnexin functions in Schizosaccharomyces pombe
Authors:Turcotte Cynthia  Roux Antoine  Beauregard Pascale B  Guérin Renée  Sénéchal Patrick  Hajjar Fadi  Rokeach Luis A
Affiliation:Department of Biochemistry, Université de Montréal, Montréal, QC, Canada.
Abstract:In the yeast Schizosaccharomyces pombe, the molecular chaperone calnexin (Cnx1p) has been shown to be essential for viability. However, we recently reported that, under certain circumstances, S. pombe cells are able to survive in the absence of calnexin/Cnx1p, indicating that an inducible pathway can complement the calnexin/Cnx1p essential function(s). This calnexin-independent state (Cin) is transmitted by a nonchromosomal proteinaceous element exhibiting several prion-like properties. To assess to what extent the Cin state compensates for the absence of calnexin/Cnx1p, the Cin strain was further characterized. Cin cells exhibited cell-wall defects, sensitivity to heat shock, as well as higher secretion levels of a model glycoprotein. Together, these results indicate that the Cin state does not compensate for all calnexin/Cnx1p functions. Reintroduction of plasmid-borne cnx1(+) partially rescued most but not all of the phenotypes displayed by Cin cells. Interestingly, Cin cells in stationary phase exhibited increased levels of caspase activation, and this phenotype was not suppressed by the reintroduction of cnx1(+), suggesting that cells in the Cin state are subjected to a stress other than the absence of calnexin/Cnx1p.
Keywords:protein folding    molecular chaperone    prion    protein secretion    fission yeast    caspases
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