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TheYarrowia lipolytica PMR1 gene (YlPMR1 ) is aSaccharomyces cerevisiae PMR1 homolog which encodes a putative secretory pathway Ca2+ -ATPase. In this study, we investigated the effects of aYlPMR1 disruption on the processing and secretion of native and foreign proteins inY. lipolytica and found variable responses by theYlPMR1 -disrupted mutant depending on the protein. The secretion of 32-kDa mature alkaline extracellular protease (AEP) was dramatically decreased, and incompletely processed precursors were observed in theYlPMR1 -disrupted mutant. A 36- and a 52-kDa premature AEP were secreted, and an intracellular 52-kDa premature AEP was also detected. The acid extracellular protease activity of theYlPMR1 -disrupted mutant was increased by 60% compared to that of the wild-type strain. The inhibitory effect of mutations in secretory pathway Ca2+ -ATPase genes on the secretion of rice α-amylase was also observed in theY. lipolytica andS. cerevisiae PMR1 -disrupted mutants. Unlike rice α-amylase, the secretion ofTrichoderma reesei endoglucanase I (EGI) was not influenced by theYlPMR1 disruption. However, the secreted EGI from theYlPMR1 -disrupted mutant had different characteristics than that of the control. While wild-type cells secreted the hyperglycosylated form of EGI, hyperglycosylation was completely absent in theYlPMR1 -disrupted mutant. Our results indicate that the effects of theYlPMR1 disruption as manifested by the phenotypic response depend on the characteristics of the reporter protein in the recombinant yeast strain evaluated.

journal of bacteriology

Disruption of PMR1 , Encoding a Ca 2+ -ATPase Homolog in Yarrowia lipolytica , Affects Secretion and Processing of Homologous and Heterologous Proteins