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J. Biol. Chem., Vol. 279, Issue 15, 14954-14960, April 9, 2004

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A Regulatory Domain in the C-terminal Extension of the Yeast Glycerol Channel Fps1p^*

Kristina Hedfalk¶, Roslyn M. Bill||, Jonathan G. L. Mullins**, Sara Karlgren, Caroline Filipsson, Johanna Bergstrom, Markus J. Tamás, Jan Rydström, and Stefan Hohmann

From the Department of Cell and Molecular Biology/Microbiology and the Department of Chemistry, Biochemistry, and Biophysics, Göteborg University and the Department of Chemistry and Bioscience/Molecular Biotechnology, Chalmers University of Technology, Box 462, 405 30 Göteborg, Sweden, the ^||School of Life and Health Sciences, Aston University, Aston Triangle, Birmingham B4 7ET, United Kingdom, and the ^**Swansea Clinical School, University of Wales Swansea, Singleton Park, Swansea SA2 8PP, United Kingdom

The Saccharomyces cerevisiae gene FPS1 encodes an aquaglyceroporin of the major intrinsic protein (MIP) family. The main function of Fps1p seems to be the efflux of glycerol in the adaptation of the yeast cell to lower external osmolarity. Fps1p is an atypical member of the family, because the protein is much larger (669 amino acids) than most MIPs due to long hydrophilic extensions in both termini. We have shown previously that a short domain in the N-terminal extension of the protein is required for restricting glycerol transport through the channel (Tamás, M. J., Karlgren, S., Bill, R. M., Hedfalk, K., Allegri, L., Ferreira, M., Thevelein, J. M., Rydström, J., Mullins, J. G. L., and Hohmann, S. (2003) J. Biol. Chem. 278, 6337–6345). Deletion of the N-terminal domain results in an unregulated channel, loss of glycerol, and osmosensitivity. In this work we have investigated the role of the Fps1p C terminus (139 amino acids). A set of eight truncations has been constructed and tested in vivo in a yeast fps1 strain. We have performed growth tests, membrane localization following cell fractionation, and glycerol accumulation measurements as well as an investigation of the osmotic stress response. Our results show that the C-terminal extension is also involved in restricting transport through Fps1p. We have identified a sequence of 12 amino acids, residues 535–546, close to the sixth transmembrane domain. This element seems to be important for controlling Fps1p function. Similar to the N-terminal domain, the C-terminal domain is amphiphilic and has a potential to dip into the membrane.

Received for publication, December 2, 2003 , and in revised form, January 28, 2004.

^* This work was supported by European Commission Grant BIO4-CT98-0024 (to S. H. and J. R.), Human Frontier Science Organization Grant QLK3-CT2000-00778 (to S. H.) and funds from the Swedish Research Council (to J. R., with a research position to S. H.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶ To whom correspondence should be addressed. Tel.: 46-31-773-3923; Fax: 46-31-773-2599; E-mail: kristina.hedfalk{at}molbiotech.chalmers.se.

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