title: Phosphatidylethanolamine is required for normal cell morphology and cytokinesis in the fission yeast Schizosaccharomyces pombe.
abstract: To investigate the contributions of phosphatidylethanolamine to the growth and morphogenesis of the fission yeast Schizosaccharomyces pombe, we have characterized three predicted genes in this organism, designated psd1, psd2, and psd3, encoding phosphatidylserine decarboxylases, which catalyze the conversion of phosphatidylserine to phosphatidylethanolamine in both eukaryotic and prokaryotic organisms. S. pombe mutants carrying deletions in any one or two psd genes are viable in complex rich medium and synthetic defined minimal medium. However, mutants carrying deletions in all three psd genes (psd1-3Delta mutants) grow slowly in rich medium and are inviable in minimal medium, indicating that the psd1 to psd3 gene products share overlapping essential cellular functions. Supplementation of growth media with ethanolamine, which can be converted to phosphatidylethanolamine by the Kennedy pathway, restores growth to psd1-3Delta cells in minimal medium, indicating that phosphatidylethanolamine is essential for S. pombe cell growth. psd1-3Delta cells produce lower levels of phosphatidylethanolamine than wild-type cells, even in medium supplemented with ethanolamine, indicating that the Kennedy pathway can only partially compensate for the loss of phosphatidylserine decarboxylase activity in S. pombe. psd1-3Delta cells appear morphologically indistinguishable from wild-type S. pombe cells in medium supplemented with ethanolamine, but when cultured in nonsupplemented medium, they produce high frequencies of abnormally shaped cells as well as cells exhibiting severe septation defects, including multiple, mispositioned, deformed, and misoriented septa. Our results demonstrate that phosphatidylethanolamine is essential for cell growth and for normal cytokinesis and cellular morphogenesis in S. pombe, and they illustrate the usefulness of this model eukaryote for investigating potentially conserved biological and molecular functions of phosphatidylethanolamine.
authors.affiliation: Department of Biological Sciences, The University of Alabama, Tuscaloosa, AL 35487, USA.
authors.forename: Jun
authors.initials: J
authors.lastname: Luo
authors.forename: Yasuhiro
authors.initials: Y
authors.lastname: Matsuo
authors.forename: Galina
authors.initials: G
authors.lastname: Gulis
authors.forename: Haylee
authors.initials: H
authors.lastname: Hinz
authors.forename: Jana
authors.initials: J
authors.lastname: Patton-Vogt
authors.forename: Stevan
authors.initials: S
authors.lastname: Marcus
mesh_terms: D000595:Amino Acid Sequence; D002262:Carboxy-Lyases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D003470:Culture Media / Q000378:metabolism; D048749:Cytokinesis; D008969:Molecular Sequence Data; D010714:Phosphatidylethanolamines / Q000378:metabolism*; D012568:Schizosaccharomyces / Q000166:cytology* / Q000201:enzymology / Q000235:genetics / Q000378:metabolism*; D029702:Schizosaccharomyces pombe Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment
chemical_list: D003470:Culture Media; D010714:Phosphatidylethanolamines; D029702:Schizosaccharomyces pombe Proteins; C483858:phosphatidylethanolamine; D002262:Carboxy-Lyases; C022353:phosphatidylserine decarboxylase