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Gene Review

CWH41  -  Cwh41p

Saccharomyces cerevisiae S288c

Synonyms: DER7, GLS1, Glucosidase I, Mannosyl-oligosaccharide glucosidase, Processing A-glucosidase I, ...
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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


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 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].


  1. The role of glucosidase I (Cwh41p) in the biosynthesis of cell wall beta-1,6-glucan is indirect. Abeijon, C., Chen, L.Y. Mol. Biol. Cell (1998) [Pubmed]
  2. Glycoprotein biosynthesis in the alg3 Saccharomyces cerevisiae mutant. I. Role of glucose in the initial glycosylation of invertase in the endoplasmic reticulum. Verostek, M.F., Atkinson, P.H., Trimble, R.B. J. Biol. Chem. (1993) [Pubmed]
  3. Early steps in processing of yeast glycoproteins. Esmon, B., Esmon, P.C., Schekman, R. J. Biol. Chem. (1984) [Pubmed]
  4. The yeast CWH41 gene encodes glucosidase I. Romero, P.A., Dijkgraaf, G.J., Shahinian, S., Herscovics, A., Bussey, H. Glycobiology (1997) [Pubmed]
  5. CWH41 encodes a novel endoplasmic reticulum membrane N-glycoprotein involved in beta 1,6-glucan assembly. Jiang, B., Sheraton, J., Ram, A.F., Dijkgraaf, G.J., Klis, F.M., Bussey, H. J. Bacteriol. (1996) [Pubmed]
  6. An improved purification procedure for soluble processing alpha-glucosidase I from Saccharomyces cerevisiae overexpressing CWH41. Faridmoayer, A., Scaman, C.H. Protein Expr. Purif. (2004) [Pubmed]
  7. DER7, encoding alpha-glucosidase I is essential for degradation of malfolded glycoproteins of the endoplasmic reticulum. Hitt, R., Wolf, D.H. FEMS Yeast Res. (2004) [Pubmed]
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