Identification and characterization of SNQ2, a new multidrug ATP binding cassette transporter of the yeast plasma membrane

• Published in: The Journal of biological chemistry 1995-07, Vol.270 (30), p.18150-18157
• Main Authors: Decottignies, A. (Universite Catholique de Louvain, Louvain-la-Neuve, Belgium.), Lambert, L, Catty, P, Degand, H, Epping, E.A, Moye-Rowley, W.S, Balzi, E, Goffeau, A
• Format: Article
• Language: English
• Subjects: ADENOSINE TRIPHOSPHATE; ADENOSINTRIFOSFATO; ADN; ATP-Binding Cassette Transporters - chemistry; ATP-Binding Cassette Transporters - genetics; ATP-Binding Cassette Transporters - metabolism; Base Sequence; Carrier Proteins - antagonists & inhibitors; Carrier Proteins - isolation & purification; Carrier Proteins - metabolism; Cell Division - genetics; Cell Membrane - metabolism; DNA Primers; DNA-Binding Proteins - metabolism; ESTRUCTURA CELULAR; Fungal Proteins - chemistry; Fungal Proteins - genetics; Fungal Proteins - isolation & purification; Fungal Proteins - metabolism; GENETICA; GENETIQUE; Hydrolysis; MEDICAMENT; MEDICAMENTOS; Membrane Proteins - antagonists & inhibitors; Membrane Proteins - isolation & purification; Membrane Proteins - metabolism; Molecular Sequence Data; PROTEINAS AGLUTINANTES; PROTEINE DE LIAISON; PURIFICACION; PURIFICATION; Pyrophosphatases - metabolism; RESISTANCE AUX PRODUITS CHIMIQUES; RESISTENCIA A PRODUCTOS QUIMICOS; SACCHAROMYCES CEREVISIAE; Saccharomyces cerevisiae - metabolism; Saccharomyces cerevisiae Proteins; STRUCTURE CELLULAIRE; TRANSCRIPCION; TRANSCRIPTION; Transcription, Genetic
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1074/jbc.270.30.18150

The SNQ2 gene of Saccharomyces cerevisiae which encodes an ATP binding cassette protein responsible for resistance to the mutagen 4-nitroquinoline oxide, is regulated by the DNA-binding proteins PDR1 and PDR3. In a plasma membrane-enriched fraction from a pdr1 mutant, the SNQ2 protein is found in the 160-kDa overexpressed band, together with PDR5. The SNQ2 protein was solubilized with n-dodecyl beta-D-maltoside from the plasma membranes of a PDR5-deleted strain and separated from the PMA1 H+-ATPase by sucrose gradient centrifugation. The enzyme shows a nucleoside triphosphatase activity that differs biochemically from that of PDR5 (Decottignies, A., Kolaczkowski, M., Balzi, E., and Goffeau, A. (1994) J. Biol. Chem. 269, 12797-12803) and is sensitive to vanadate, erythrosine B, and Triton X-100 but not to oligomycin, which inhibits the PDR5 activity only. Disruption of both PDR5 and SNQ2 in a pdr1 mutant decreases the cell growth rate and reveals the presence of at least two other ATP binding cassette proteins in the 160-kDa overexpressed band that have been identified by amino-terminal microsequencing