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1: J Biol Chem. 1994 Apr 29;269(17):12797-803.Click here to read Links

Solubilization and characterization of the overexpressed PDR5 multidrug resistance nucleotide triphosphatase of yeast.

Decottignies A, Kolaczkowski M, Balzi E, Goffeau A.

Unité de Biochimie Physiologique, Université Catholique de Louvain, Louvain-la-Neuve, Belgium.

A 160-kDa plasma membrane protein of the yeast Saccharomyces cerevisiae was overexpressed by mutating the PDR1 or the PDR3 transcription factor gene. The protein is the membrane-bound ATP binding cassette transporter PDR5 (Balzi, E., Wang, M., Leterme, S., Van Dyck, L., and Goffeau, A. (1994) J. Biol. Chem. 269, 2206-2214). PDR5 was solubilized with n-dodecyl-beta-D-malto-side and separated from the PMA1 plasma membrane H(+)-ATPase by glycerol gradient centrifugation. The PDR5 protein hydrolyzes nucleoside diphosphates and triphosphates. This activity is sensitive to low concentrations of vanadate, of oligomycin, and of a variety of hydrophobic compounds. Many of these properties liken PDR5 to the purified mammalian P-glycoprotein responsible for multidrug resistance.

PMID: 8175692 [PubMed - indexed for MEDLINE]