ArticleCurrent microbiology2007
Influence of N-glycosylation on Saccharomyces cerevisiae morphology: a golgi glycosylation mutant shows cell division defects.
Article in Current microbiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed.
- Recent Advances Toward Engineering Glycoproteins Using Modified Yeast Display Platforms.Methods in molecular biology (Clifton, N.J.) · 2022Review
- Expression and Display of Glycoengineered Antibodies and Antibody Fragments with an Engineered Yeast Strain.Antibodies (Basel, Switzerland) · 2021Article
- Article
- Knockout of an endogenous mannosyltransferase increases the homogeneity of glycoproteins produced in Pichia pastoris.Scientific reports · 2013Article
- PCR on yeast colonies: an improved method for glyco-engineered Saccharomyces cerevisiae.BMC research notes · 2013Article
- Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
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).
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Registered trials
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