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Vol. 11, Issue 2, 435-452, February 2000
Department of Molecular, Cellular, and Developmental Biology, Yale
University, New Haven, Connecticut 06520-8103
The cell wall of fungal cells is important for cell integrity and
cell morphogenesis and protects against harmful environmental conditions. The yeast cell wall is a complex structure consisting mainly of mannoproteins, glucan, and chitin. The molecular mechanisms by which the cell wall components are synthesized and transported to
the cell surface are poorly understood. We have identified and
characterized two homologous yeast proteins, Sbe2p and Sbe22p, through
their suppression of a chs5 spa2 mutant strain defective in chitin synthesis and cell morphogenesis. Although
sbe2 and sbe22 null mutants are viable,
sbe2 sbe22 cells display several phenotypes indicative
of defects in cell integrity and cell wall structure. First,
sbe2 sbe22 cells display a sorbitol-remediable lysis
defect at 37°C and are hypersensitive to SDS and calcofluor. Second,
electron microscopic analysis reveals that sbe2 sbe22 cells have an aberrant cell wall structure with a reduced mannoprotein layer. Finally, immunofluorescence experiments reveal that in small-budded cells, sbe2 sbe22 mutants mislocalize
Chs3p, a protein involved in chitin synthesis. In addition, sbe2
sbe22 diploids have a bud-site selection defect, displaying a
random budding pattern. A Sbe2p-GFP fusion protein localizes to
cytoplasmic patches, and Sbe2p cofractionates with Golgi proteins.
Deletion of CHS5, which encodes a Golgi protein involved
in the transport of Chs3p to the cell periphery, is lethal in
combination with disruption of SBE2 and
SBE22. Thus, we suggest a model in which Sbe2p and Sbe22p are involved in the transport of cell wall components from the
Golgi apparatus to the cell surface periphery in a pathway independent
of Chs5p.
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