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

被引:5
|
作者
Xu, Xin-Xin [1 ,2 ]
Komatsuzaki, Akiko [2 ]
Chiba, Yasunori [2 ]
Gao, Xiao-Dong [1 ]
Yoko-o, Takehiko [2 ]
机构
[1] Jiangnan Univ, Minist Educ, Key Lab Carbohydrate Chem & Biotechnol, Wuxi 214122, Peoples R China
[2] Natl Inst Adv Ind Sci & Technol, Biotechnol Res Inst Drug Discovery, Tsukuba, Ibaraki 3058568, Japan
基金
日本学术振兴会;
关键词
GAS1; GPI anchor; lipid remodelling; Ogataea minuta; GPI-ANCHORED PROTEINS; GLYCOSYLPHOSPHATIDYLINOSITOL MEMBRANE ANCHORS; SACCHAROMYCES-CEREVISIAE; INOSITOL DEACYLATION; BETA-HEXOSAMINIDASE; PLASMA-MEMBRANE; ER EXIT; BIOSYNTHESIS; CERAMIDES; IDENTIFICATION;
D O I
10.1002/yea.3285
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 per1 mutant exhibited a more fragile phenotype than the gup1 or cwh43 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 per1 or gup1 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.
引用
收藏
页码:225 / 236
页数:12
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