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Genetics, Vol. 158, 1397-1411, August 2001, Copyright © 2001

Coordination Between Fission Yeast Glucan Formation and Growth Requires a Sphingolipase Activity

Anna Feoktistovaa, Paula Magnellic, Claudia Abeijonc, Pilar Perezd, Robert L. Lestere, Robert C. Dicksone, and Kathleen L. Goulda,b
a Howard Hughes Medical Institute, Vanderbilt University School of Medicine, Nashville, Tennessee 37232,
b Department of Cell Biology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232,
c Department of Molecular and Cell Biology, Boston University-Goldman School of Dental Medicine, Boston, Massachusetts 02118,
d Instituto de Microbiologia Bioquimica, CSIC, Universidad de Salamanca, Edificio Departmental, 37007 Salamanca, Spain
e Department of Biochemistry and the Lucille P. Markey Cancer Center, University of Kentucky College of Medicine, Lexington, Kentucky 40536-0096

Corresponding author: Kathleen L. Gould, HHMI and Department of Cell Biology, B2309 MCN, Vanderbilt University School of Medicine, 1161 21st Ave. S., Nashville, TN 37232., kathy.gould{at}mcmail.vanderbilt.edu (E-mail)

Communicating editor: P. RUSSELL

css1 mutants display a novel defect in Schizosaccharomyces pombe cell wall formation. The mutant cells are temperature-sensitive and accumulate large deposits of material that stain with calcofluor and aniline blue in their periplasmic space. Biochemical analyses of this material indicate that it consists of {alpha}- and ß-glucans in the same ratio as found in cell walls of wild-type S. pombe. Strikingly, the glucan deposits in css1 mutant cells do not affect their overall morphology. The cells remain rod shaped, and the thickness of their walls is unaltered. Css1p is an essential protein related to mammalian neutral sphingomyelinase and is responsible for the inositolphosphosphingolipid-phospholipase C activity observed in S. pombe membranes. Furthermore, expression of css1+ can compensate for loss of ISC1, the enzyme responsible for this activity in Saccharomyces cerevisiae membranes. Css1p localizes to the entire plasma membrane and secretory pathway; a C-terminal fragment of Css1p, predicted to encode a single membrane-spanning segment, is sufficient to direct membrane localization of the heterologous protein, GFP. Our results predict the existence of an enzyme(s) or process(es) essential for the coordination of S. pombe cell wall formation and division that is, in turn, regulated by a sphingolipid metabolite.




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