Influence of N-Glycosylation on Saccharomyces cerevisiae Morphology: A Golgi Glycosylation Mutant Shows Cell Division Defects

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• 作者：Jungang Zhou ; Houcheng Zhang ; Xianwei Liu ; Peng George Wang and Qingsheng Qi
• 关键词：Cell division ; Glycosylation ; Morphology ; Mutant ; Yeast
• 刊名：Current Microbiology
• 出版年：2007
• 出版时间：September, 2007
• 年：2007
• 卷：55
• 期：3
• 页码：198-204
• 全文大小：186 KB

文摘

The N-glycosylation mutants (mnn1 and mnn1 och1) show different morphological characteristics at the restrictive and nonpermissive temperature. We deleted the MNN1 to eliminate the terminal α1, 3-linked mannose of hypermannosylation and deleted the OCH1 to block the elongation of the main backbone chain. The mnn1 cells exhibited no observable change with respect to the wild-type strain at 28¡ãC and 37¡ãC, but the mnn1 och1 double mutant exhibited defects in cell cytokinesis, showed a slower growth rate, and became temperature-sensitive. Meanwhile, the mnn1 och1 mutant tended to aggregate, which was probably due to the glycolsylation defect. Loss of mannosyl-phosphate-accepting sites in this mutant migth result in reduced charge repulsion between cell surfaces. Pyridylaminated glycans were profiled and purified through an NH₂ column by size-fractionation high-performance liquid chromatography. Matrix assisted laser desoption/ionization time of flight mass spectrometry (MALDI TOF/MS) analysis of the N-glycan structure of the mnn1 och1 mutant revealed that the main component is Man₈GlcNAc₂.