High impact information on CWH41

• CWH41, a gene involved in the assembly of cell wall beta-1,6-glucan, has recently been shown to be the structural gene for Saccharomyces cerevisiae glucosidase I that is responsible for initiating the trimming of terminal alpha-1,2-glucose residue in the N-glycan processing pathway [1].
• To distinguish between a direct or indirect role of Cwh41p in the biosynthesis of beta-1,6-glucan, we constructed a double mutant, alg5Delta (lacking dolichol-P-glucose synthase) cwh41Delta, and found that it has the same phenotype as the alg5Delta single mutant [1].
• Therefore, an alg3,sec18,gls1 strain was constructed to delete the GLS1-encoded glucosidase I responsible for trimming the terminal alpha 1,2-linked glucose from newly transferred Glc3ManxGlcNAc2 oligosaccharides [2].
• When transport from the endoplasmic reticulum is blocked in sec18, N-linked oligosaccharides accumulate with a size corresponding to Man8GlcNAc2 when the normal GLS1 allele is present, and Glc3Man8GlcNAc2 in the gls1 mutant [3].
• Tetrad analysis for glucosidase I activity in vitro and in vivo was done on the progeny from the spores obtained from the heterozygous diploid, cwh41 delta::HIS3 [4].

Biological context of CWH41

• Disruption of the CWH41 gene leads to a K1 killer toxin-resistant phenotype and a 50% reduction in the cell wall beta 1,6-glucan level [5].

Anatomical context of CWH41

• CWH41 encodes a novel endoplasmic reticulum membrane N-glycoprotein involved in beta 1,6-glucan assembly [5].

Associations of CWH41 with chemical compounds

• It is shown that, unlike CWH41 cells, cell extracts obtained from cwh41 delta null mutants are unable to release glucose residues from the synthetic trisaccharide substrate alpha-D-Glc 1-->2 alpha-D-Glc 1-->3 alpha-D-Glc-O(CH2)8 COOCH3 in vitro [4].
• Processing alpha-glucosidase I, which is encoded by CWH41, regulates one of the key steps in asparagine-linked glycoprotein biosynthesis by cleaving the terminal alpha-1,2-linked glucose from Glc(3)Man(9)GlcNAc(2), the common oligosaccharide precursor [6].
• We identify DER7 as the gene encoding N-glycan-processing alpha-glucosidase I (EC 3.2.1.106) of the ER and demonstrate that its inactivity, due to a substitution of the conserved glycine residue at position 725 by arginine (G725R) in the der7-1 mutant, leads to ER-stress [7].

References