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Volume 271, Number 23, Issue of June 7, 1996 pp. 13746-13753
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Comparative Topology Studies in Saccharomyces cerevisiae and in Escherichia coli
THE N-TERMINAL HALF OF THE YEAST ABC PROTEIN Ste6

(Received for publication, November 1, 1995, and in revised form, January 29, 1996)

Dorit Geller , Daniel Taglicht ^§ , Rotem Edgar , Amy Tam ^§ , Ophry Pines ^¶ , Susan Michaelis ^§ and Eitan Bibi

From the  Department of Biochemistry, Weizmann Institute of Science, Rehovot 76100, Israel, the ^§ Department of Cell Biology and Anatomy, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, and the ^¶ Department of Molecular Biology, The Hebrew University-Hadassah Medical School, Jerusalem 91010, Israel

Gene fusions have provided a strategy for determining the topology of polytopic membrane proteins in Escherichia coli. To evaluate whether this highly effective approach is applicable to heterologously expressed eukaryotic integral membrane proteins, we have carried out a comparative topological study of the eukaryotic membrane protein Ste6 both in bacteria and in yeast. Ste6, is an ATP binding cassette (ABC) protein, essential for export of the a-factor mating pheromone in Saccharomyces cerevisiae. The topogenic reporters, invertase in S. cerevisiae and alkaline phosphatase in E. coli, were fused to Ste6 at identical sites and the fusions were expressed in yeast and bacteria, respectively. The results obtained in both systems are similar, although more definitive in E. coli, and support the predicted six-transmembrane spans organization of the N-terminal half of Ste6. Thus, the topological determinants for membrane insertion of polytopic proteins in prokaryotic and in eukaryotic systems appear to be highly similar. In this study we also demonstrate that Ste6 does not contain a cleaved signal sequence.

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