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Eukaryotic Cell, February 2004, p. 27-39, Vol. 3, No. 1
1535-9778/04/$08.00+0     DOI: 10.1128/EC.3.1.27-39.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

ADAM Family Protein Mde10 Is Essential for Development of Spore Envelopes in the Fission Yeast Schizosaccharomyces pombe

Tomohiro Nakamura,1 Hiroko Abe,2,{dagger} Aiko Hirata,3 and Chikashi Shimoda2*

Faculty of Intellectual Property, Osaka Institute of Technology, Asahi-ku, Osaka 535-8585,1 Department of Biology, Graduate School of Science, Osaka City University, Sumiyoshi-ku, Osaka 558-8585,2 Department of Integrated Biosciences, Graduate School of Frontier Science, University of Tokyo, Kashiwa, Chiba 277-8562, Japan3

Received 12 August 2003/ Accepted 11 November 2003

We report the identification of Schizosaccharomyces pombe mde10+ as a gene possessing a FLEX element, which forms a binding site for the meiosis-specific transcription factor Mei4. In fact, mde10+ is transcribed only in diploid cells that are induced to meiosis in a Mei4-dependent manner. Western blot analysis indicated that the epitope-tagged Mde10 protein accumulates transiently during meiosis and then rapidly decreases. Mde10 is a multidomain protein containing a metalloprotease catalytic domain, a disintegrin domain, a cysteine-rich domain, and membrane-spanning regions, all of which are shared by members of the mammalian ADAM family. A fusion protein of Mde10 and green fluorescent protein localized to the endoplasmic reticulum during meiosis and was located at the peripheral region of spores at the end of meiosis. An mde10{Delta} deletion mutant showed no apparent defects in meiosis, sporulation, or spore germination. However, the mutant spores exhibited an aberrant surface appearance, in which the ragged outer spore wall was lost to a large extent. Furthermore, mde10{Delta} spores were found to be less tolerant to ethanol and diethyl ether than were wild-type spores. The mutagenic replacement of the conserved glutamic acid in the putative protease active site with an alanine residue did not affect the surface morphology or the resistance of spores to environmental stress. Our observations indicate that Mde10 is important in the development of the spore envelope, although this function of Mde10 seems to be independent of its metalloprotease activity.

* Corresponding author. Mailing address: Department of Biology, Graduate School of Science, Osaka City University, 3-3-138 Sugimoto, Sumiyoshi-ku, Osaka 558-8585, Japan. Phone: 81 66605 2576. Fax: 81 66605 3158. E-mail: shimoda{at}sci.osaka-cu.ac.jp.

{dagger} Present address: Department of Cell Regulation, Faculty of Medicine, Kagawa University, Ikenobe, Kita-gun, Kagawa 761-0795, Japan.

Eukaryotic Cell, February 2004, p. 27-39, Vol. 3, No. 1
1535-9778/04/$08.00+0     DOI: 10.1128/EC.3.1.27-39.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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