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Science 10 April 1992:
Vol. 256. no. 5054, pp. 232 - 234
DOI: 10.1126/science.1348873
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Articles

Science, Vol 256, Issue 5054, 232-234
Copyright © 1992 by American Association for the Advancement of Science

articles

Functional complementation of yeast ste6 by a mammalian multidrug resistance mdr gene

M Raymond, P Gros, M Whiteway, and DY Thomas

National Research Council of Canada, Biotechnology Research Institute, Montreal, Quebec.

Multidrug resistance in mammalian tumor cells is associated with the overexpression of mdr genes encoding P-glycoproteins, which function as drug efflux pumps. A yeast homolog of mdr, STE6, mediates export of a-factor mating peptide. Yeast MATa cells carrying a ste6 deletion produce no extracellular a-factor and therefore are defective in mating. Expression of a complementary DNA for the mouse mdr3 gene in a yeast ste6 deletion strain restored ability to export a-factor and to mate. A mutation (a serine to phenylalanine substitution at amino acid 939) known to affect the activity of the mdr3 gene product abolished its ability to complement the yeast ste6 deletion. Thus, functions of P-glycoproteins in normal mammalian cells may include the transmembrane export of endogenous peptides.


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