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. 1996 Feb;178(4):1162–1171. doi: 10.1128/jb.178.4.1162-1171.1996

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

B Jiang 1, J Sheraton 1, A F Ram 1, G J Dijkgraaf 1, F M Klis 1, H Bussey 1
PMCID: PMC177780  PMID: 8576053

Abstract

CWH41 encodes a novel type II integral membrane N-glycoprotein located in the endoplasmic reticulum. 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. CWH41 also displays strong genetic interactions with KRE1 and KRE6, two genes known to be involved in the beta 1,6-glucan biosynthetic pathway. The cwh41 delta kre6 delta double mutant is nonviable; and the cwh41 delta kre1 delta double mutation results in strong synergistic defects, with a severely slow-growth phenotype, a 75% reduction in beta 1,6-glucan level, and the secretion of a cell wall glucomannoprotein, Cwp1p. These results provide strong genetic evidence indicating that Cwh41p plays a functional role, possibly as a new synthetic component, in the assembly of cell wall beta 1,6-glucan.

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Selected References

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