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-1,6-Glucan Is Indirect
Department of Molecular and Cell Biology, Boston University-Goldman
School of Dental Medicine, Boston, Massachusetts 02118
CWH41, a gene involved in the assembly of cell wall
-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 
-1,2-glucose
residue in the N-glycan processing pathway. To distinguish
between a direct or indirect role of Cwh41p in the biosynthesis of
-1,6-glucan, we constructed a double mutant, alg5
(lacking dolichol-P-glucose synthase) cwh41, and
found that it has the same phenotype as the alg5
single mutant. It contains wild-type levels of cell wall
-1,6-glucan, shows moderate underglycosylation of N-linked
glycoproteins, and grows at concentrations of Calcofluor White (which
interferes with cell wall assembly) that are lethal to
cwh41 single mutant. The strong genetic interactions of CWH41 with KRE6 and
KRE1, two other genes involved in the -1,6-glucan biosynthetic pathway, disappear in the absence of dolichol-P-glucose synthase (alg5). The triple mutant
alg5cwh41kre6 is viable, whereas the double
mutant cwh41kre6 in the same genetic background is
not. The severe slow growth phenotype and 75% reduction in cell wall
-1,6-glucan, characteristic of the cwh41kre1
double mutant, are not observed in the triple mutant
alg5cwh41kre1. Kre6p, a putative Golgi glucan
synthase, is unstable in cwh41 strains, and its overexpression
renders these cells Calcofluor White resistant. These results
demonstrate that the role of glucosidase I (Cwh41p) in the biosynthesis
of cell wall -1,6-glucan is indirect and that dolichol-P-glucose is
not an intermediate in this pathway.
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