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Eukaryotic Cell, October 2004, p. 1124-1135, Vol. 3, No. 5
1535-9778/04/$08.00+0     DOI: 10.1128/EC.3.5.1124-1135.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Schizosaccharomyces pombe Pmr1p Is Essential for Cell Wall Integrity and Is Required for Polarized Cell Growth and Cytokinesis

Juan Carlos G. Cortés,1 Reiko Katoh-Fukui,2 Kanako Moto,2 Juan Carlos Ribas,1 and Junpei Ishiguro2*

Instituto de Microbiología Bioquímica and Departamento de Microbiología y Genética, Consejo Superior de Investigaciones Científicas (CSIC)/Universidad de Salamanca, Salamanca, Spain,1 Department of Biology, Faculty of Science and Engineering, Konan University, Okamoto, Kobe, Japan2

Received 18 March 2004/ Accepted 22 June 2004

The cps5-138 fission yeast mutant shows an abnormal lemon-like morphology at 28°C in minimal medium and a lethal thermosensitive phenotype at 37°C. Cell growth is completely inhibited at 28°C in a Ca2+-free medium, in which the wild type is capable of growing normally. Under these conditions, actin patches become randomly distributed throughout the cell, and defects in septum formation and subsequent cytokinesis appear. The mutant cell is hypersensitive to the cell wall-digesting enzymatic complex Novozym234 even under permissive conditions. The gene SPBC31E1.02c, which complements all the mutant phenotypes described above, was cloned and codes for the Ca2+-ATPase homologue Pmr1p. The gene is not essential under optimal growth conditions but is required under conditions of low Ca2+ (<0.1 mM) or high temperature (>35°C). The green fluorescent protein-tagged Cps5 proteins, which are expressed under physiological conditions (an integrated single copy with its own promoter in the cps5{Delta} strain), display a localization pattern typical of endoplasmic reticulum proteins. Biochemical analyses show that 1,3-ß-D-glucan synthase activity in the mutant is decreased to nearly half that of the wild type and that the mutant cell wall contains no detectable galactomannan when the cells are exposed to a Ca2+-free medium. The mutant acid phosphatase has an increased electrophoretic mobility, suggesting that incomplete protein glycosylation takes place in the mutant cells. These results indicate that S. pombe Pmr1p is essential for the maintenance of cell wall integrity and cytokinesis, possibly by allowing protein glycosylation and the polarized actin distribution to take place normally. Disruption and complementation analyses suggest that Pmr1p shares its function with a vacuolar Ca2+-ATPase homologue, Pmc1p (SPAPB2B4.04c), to prevent lethal activation of calcineurin for cell growth.

* Corresponding author. Mailing address: Department of Biology, Faculty of Science and Engineering, Konan University, Okamoto 8-9-1, Kobe 658-8501, Japan. Phone: 81-78-435-2516. Fax: 81-78-435-2539. E-mail: ishiguro{at}konan-u.ac.jp.

Eukaryotic Cell, October 2004, p. 1124-1135, Vol. 3, No. 5
1535-9778/04/$08.00+0     DOI: 10.1128/EC.3.5.1124-1135.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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