Eukaryotic Cell
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Eukaryotic Cell, November 2007, p. 2092-2101, Vol. 6, No. 11
1535-9778/07/$08.00+0     doi:10.1128/EC.00300-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Functional Characterization of the Fission Yeast Phosphatidylserine Synthase Gene, pps1, Reveals Novel Cellular Functions for Phosphatidylserine{triangledown}

Yasuhiro Matsuo,1 Edward Fisher,2 Jana Patton-Vogt,2 and Stevan Marcus1*

Department of Biological Sciences, The University of Alabama, Tuscaloosa, Alabama 35487,1 Department of Biological Sciences, Duquesne University, Pittsburgh, Pennsylvania 152822

Received 15 August 2007/ Accepted 18 September 2007

To investigate the contributions of phosphatidylserine to the growth and morphogenesis of the rod-shaped fission yeast Schizosaccharomyces pombe, we have characterized the single gene in this organism, pps1, encoding a predicted phosphatidylserine synthase. S. pombe pps1{Delta} mutants grow slowly in rich medium and are inviable in synthetic minimal medium. They do not produce detectable phosphatidylserine in vivo and possess negligible in vitro phosphatidylserine synthase activity, indicating that pps1 encodes the major phosphatidylserine synthase activity in S. pombe. Supplementation of growth medium with ethanolamine partially suppresses the growth-defective phenotype of pps1{Delta} cells, reflecting the likely importance of phosphatidylserine as a precursor for phosphatidylethanolamine in S. pombe. In medium lacking ethanolamine, pps1{Delta} mutants exhibit striking cell morphology, cytokinesis, actin cytoskeleton, and cell wall remodeling and integrity defects. Overexpression of pps1 likewise leads to defects in cell morphology and cytokinesis, thus implicating phosphatidylserine as a dosage-dependent regulator of these processes. During log-phase growth, green fluorescent protein-Pps1p fusion proteins are concentrated at the cell and nuclear peripheries as well as presumptive endoplasmic reticulum membranes, while in stationary-phase cells, they are redistributed to unusual cytoplasmic structures of unknown origin. Moreover, stationary-phase pps1{Delta} cultures retain very poor viability relative to wild-type S. pombe cells, even in medium containing ethanolamine, demonstrating a role for phosphatidylserine in the physiological adaptations required for stationary-phase survival. Our findings reveal novel cellular functions for phosphatidylserine and emphasize the usefulness of S. pombe as a model organism for elucidating potentially conserved biological and molecular functions of this phospholipid.

* Corresponding author. Mailing address: Dept. of Biological Sciences, The University of Alabama, 343A Shelby Hall, 250 Hackberry Lane, Box 870336, Tuscaloosa, AL 35487. Phone: (205) 348-8094. Fax: (205) 348-9104. E-mail: smarcus{at}bama.ua.edu

{triangledown} Published ahead of print on 28 September 2007.

Eukaryotic Cell, November 2007, p. 2092-2101, Vol. 6, No. 11
1535-9778/07/$08.00+0     doi:10.1128/EC.00300-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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