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Vol. 9, Issue 6, 1565-1576, June 1998
Department of Molecular and Cell Biology, Howard Hughes Medical
Institute, University of California, Berkeley, Berkeley, California
94720
Chitin synthase III (CSIII), an enzyme required to form a chitin
ring in the nascent division septum of Saccharomyces
cerevisiae, may be transported to the cell surface in a
regulated manner. Chs3p, the catalytic subunit of CSIII, requires the
product of CHS6 to be transported to or activated at the
cell surface. We find that chs6
strains have
morphological abnormalities similar to those of chs3
mutants. Subcellular fractionation and indirect immunofluorescence
indicate that Chs3p distribution is altered in chs6
mutant cells. Order-of-function experiments using
end4-1 (endocytosis-defective) and chs6
mutants indicate that Chs6p is required for anterograde transport of
Chs3p from an internal endosome-like membrane compartment, the
chitosome, to the plasma membrane. As a result, chs6
strains accumulate Chs3p in chitosomes. Chs1p, a distinct chitin
synthase that acts during or after cell separation, is transported
normally in chs6 mutants, suggesting that Chs1p and
Chs3p are independently packaged during protein transport through the
late secretory pathway.
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