Decottignies, Anabelle
[UCL]
Kolaczkowski, M
Balzi, E.
Goffeau, André
[UCL]
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.
Référence bibliographique |
Decottignies, Anabelle ; Kolaczkowski, M ; Balzi, E. ; Goffeau, André. Solubilization and characterization of the overexpressed PDR5 multidrug resistance nucleotide triphosphatase of yeast.. In: The Journal of biological chemistry, Vol. 269, no. 17, p. 12797-803 (1994) |
Permalien |
http://hdl.handle.net/2078.1/12025 |