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J Bacteriol, April 1998, p. 1700-1708, Vol. 180, No. 7
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

The Saccharomyces cerevisiae SCS2 Gene Product, a Homolog of a Synaptobrevin-Associated Protein, Is an Integral Membrane Protein of the Endoplasmic Reticulum and Is Required for Inositol Metabolism

Satoshi Kagiwada,1,* Kohei Hosaka,2 Masayuki Murata,3 Jun-ichi Nikawa,4 and Akira Takatsuki1

Animal and Cellular Systems Laboratory, The Institute of Physical and Chemical Research (RIKEN), Wako, Saitama 351-01,1 Department of Basic Allied Medicine, Gunma University School of Health Sciences, Maebashi 371,2 Ultrastructural Research Laboratory, National Institute for Physiological Sciences, Okazaki, Aichi 444,3 and Department of Biochemical Engineering and Science, Faculty of Computer Science and Systems Engineering, Kyushu Institute of Technology, Iizuka, Fukuoka 820,4 Japan

Received 8 October 1997/Accepted 20 January 1998

The Saccharomyces cerevisiae SCS2 gene has been cloned as a suppressor of inositol auxotrophy of CSE1 and hac1/ire15 mutants (J. Nikawa, A. Murakami, E. Esumi, and K. Hosaka, J. Biochem. 118:39-45, 1995) and has homology with a synaptobrevin/VAMP-associated protein, VAP-33, cloned from Aplysia californica (P. A. Skehel, K. C. Martin, E. R. Kandel, and D. Bartsch, Science 269:1580-1583, 1995). In this study we have characterized an SCS2 gene product (Scs2p). The product has a molecular mass of 35 kDa and is C-terminally anchored to the endoplasmic reticulum, with the bulk of the protein located in the cytosol. The disruption of the SCS2 gene causes yeast cells to exhibit inositol auxotrophy at temperatures of above 34°C. Genetic studies reveal that the overexpression of the INO1 gene rescues the inositol auxotrophy of the SCS2 disruption strain. The significant primary structural feature of Scs2p is that the protein contains the 16-amino-acid sequence conserved in yeast and mammalian cells. The sequence is required for normal Scs2p function, because a mutant Scs2p that lacks the sequence does not complement the inositol auxotrophy of the SCS2 disruption strain. Therefore, the Scs2p function might be conserved among eukaryotic cells.

* Corresponding author. Present address: Department of Biology, Nara Women's University, Nara 630, Japan. Phone and fax: 81-742-20-3416.




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