In eukaryotes, the glycosylphosphatidylinositol (GPI) modification of many 
glycoproteins on the cell surface is highly conserved. The lipid moieties of 
GPI-anchored proteins undergo remodelling 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 remodelling. Here, we 
focus on the putative GPI remodelling pathway in the methylotrophic yeast 
Ogataea minuta. We found that the O. minuta homologues 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 homologues 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 remodelling for GPI-anchored proteins in O. 
minuta. Localization behaviour of Gas1Bp differed from that of Gas1Ap. Our data 
reveals, for the first time (to our knowledge), the existence of genes related 
to GPI anchor remodelling in O. minuta cells.