PER1, GUP1, and CWH43 of methylotrophic yeast Ogataea minuta are involved in cell wall integrity

SUMMARY In eukaryotes, the glycosylphosphatidylinositol (GPI) modification of many glycoproteins on the cell surface is highly conserved. The lipid moieties of GPI‐anchored proteins undergo remodeling processes during their maturation. To date, the products of the PER1, GUP1, and CWH43 genes of the yeast Saccharomyces cerevisiae have been shown to be involved in the lipid remodeling. Here, we focus on the putative GPI remodeling pathway in the methylotrophic yeast Ogataea minuta. We found that the O. minuta homologs of PER1, GUP1, and CWH43 are functionally compatible with those of S. cerevisiae. Disruption of GUP1 or CWH43 in O. minuta caused a growth defect under non‐permissive conditions. The O. minuta per1Δ mutant exhibited a more fragile phenotype than the gup1Δ or cwh43Δ mutants. To address the role of GPI modification in O. minuta, we assessed the effect of these mutations on the processing and localization of the O. minuta homologs of the Gas1 protein; in S. cerevisiae, Gas1p is an abundant and well‐characterized GPI‐anchored protein. We found that O. minuta possesses two copies of the GAS1 gene, which we designate GAS1A and GAS1B. Microscopy and western blotting analysis showed mislocalization and/or lower retention of Gas1Ap and Gas1Bp within the membrane fraction in per1Δ or gup1Δ mutant cells, suggesting the significance of lipid remodeling for GPI‐anchored proteins in O. minuta. Localization behavior of Gas1Bp differed from that of Gas1Ap. Our data...
Source: Yeast - Category: Molecular Biology Authors: Tags: RESEARCH ARTICLE Source Type: research