Reference: Zhou J, et al. (2007) Influence of N-glycosylation on Saccharomyces cerevisiae morphology: a golgi glycosylation mutant shows cell division defects. Curr Microbiol 55(3):198-204

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Abstract


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 alpha1, 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 degrees C and 37 degrees C, 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 NH(2) 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 Man(8)GlcNAc(2).

Reference Type
Journal Article | Research Support, Non-U.S. Gov't
Authors
Zhou J, Zhang H, Liu X, Wang PG, Qi Q
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