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A yeast homologue of the bovine lens fibre MIP gene family complements the growth defect of a Saccharomyces cerevisiae mutant on fermentable sugars but not its defect in glucose-induced RAS-mediated cAMP signalling.

1991; Springer Nature; Volume: 10; Issue: 8 Linguagem: Inglês

10.1002/j.1460-2075.1991.tb07742.x

1460-2075

Linda Van Aelst, Stefan Hohmann, F. K. Zimmermann, A. W. H. Jans, Johan M. Thevelein,

Polyamine Metabolism and Applications

Research Article1 August 1991free access A yeast homologue of the bovine lens fibre MIP gene family complements the growth defect of a Saccharomyces cerevisiae mutant on fermentable sugars but not its defect in glucose-induced RAS-mediated cAMP signalling. L. Van Aelst L. Van Aelst Laboratorium voor Cellulaire Biochemie, Katholieke Universiteit te Leuven, Leuven-Heverlee, Flanders, Belgium. Search for more papers by this author S. Hohmann S. Hohmann Laboratorium voor Cellulaire Biochemie, Katholieke Universiteit te Leuven, Leuven-Heverlee, Flanders, Belgium. Search for more papers by this author F.K. Zimmermann F.K. Zimmermann Laboratorium voor Cellulaire Biochemie, Katholieke Universiteit te Leuven, Leuven-Heverlee, Flanders, Belgium. Search for more papers by this author A.W. Jans A.W. Jans Laboratorium voor Cellulaire Biochemie, Katholieke Universiteit te Leuven, Leuven-Heverlee, Flanders, Belgium. Search for more papers by this author J.M. Thevelein J.M. Thevelein Laboratorium voor Cellulaire Biochemie, Katholieke Universiteit te Leuven, Leuven-Heverlee, Flanders, Belgium. Search for more papers by this author L. Van Aelst L. Van Aelst Laboratorium voor Cellulaire Biochemie, Katholieke Universiteit te Leuven, Leuven-Heverlee, Flanders, Belgium. Search for more papers by this author S. Hohmann S. Hohmann Laboratorium voor Cellulaire Biochemie, Katholieke Universiteit te Leuven, Leuven-Heverlee, Flanders, Belgium. Search for more papers by this author F.K. Zimmermann F.K. Zimmermann Laboratorium voor Cellulaire Biochemie, Katholieke Universiteit te Leuven, Leuven-Heverlee, Flanders, Belgium. Search for more papers by this author A.W. Jans A.W. Jans Laboratorium voor Cellulaire Biochemie, Katholieke Universiteit te Leuven, Leuven-Heverlee, Flanders, Belgium. Search for more papers by this author J.M. Thevelein J.M. Thevelein Laboratorium voor Cellulaire Biochemie, Katholieke Universiteit te Leuven, Leuven-Heverlee, Flanders, Belgium. Search for more papers by this author Author Information L. Van Aelst1, S. Hohmann1, F.K. Zimmermann1, A.W. Jans1 and J.M. Thevelein1 1Laboratorium voor Cellulaire Biochemie, Katholieke Universiteit te Leuven, Leuven-Heverlee, Flanders, Belgium. The EMBO Journal (1991)10:2095-2104https://doi.org/10.1002/j.1460-2075.1991.tb07742.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Recently a new family of membrane proteins comprising the bovine lens fibre major intrinsic protein, soybean nodulin-26 protein and the Escherichia coli glycerol facilitator has been described [M.E. Baker and M.H. Saier, Jr (1990) Cell, 60, 185–186]. These proteins have six putative membrane spanning domains and one (probably intracellular) intermembrane fragment is particularly well conserved. We have identified a new member of this family in the yeast Saccharomyces cerevisiae. It also possesses the six transmembrane domains and the highly conserved intermembrane sequence. In contrast to the other three proteins which are all approximately 280 amino acids long, the yeast protein has an N-terminal extension of approximately 250 amino acids, which contains a string of 17 asparagine residues and a C-terminal extension of approximately 150 amino acids. The gene, which we called FPS1 (for fdp1 suppressor), suppresses in single copy the growth defect on fermentable sugars of the yeast fdp1 mutant but it is not allelic to FDP1. The deficiency of the fdp1 mutant in glucose-induced RAS-mediated cAMP signalling and in rapid glucose-induced changes in the activity of certain enzymes was not restored. Deletion of FPS1 does not cause any of the phenotypic deficiencies of the fdp1 mutant. Previous ArticleNext Article Volume 10Issue 81 August 1991In this issue RelatedDetailsLoading ...