Abstract
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 over-expressed 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.
Highlights
The SNQ2 gene of Saccharomyces cerevzszae, which encodes an ATP binding cassette protein responsible for resistance to the mutagen 4·nitroquinoline oxide, is re· gulated by the DNA-binding proteins PDR1 and PDR3
The SNQ2 protein was solubilized with n-dodecyl f.'l-o-maltoside from the plasma membranes of a PDR5-deleted strain and separated from the PMA1 H+-ATPase by sucrose gradient centrifugation
MATa, PDRJ, PDR5, SNQ2, hisl, parental of DRI9-T8 MATa, pdrl-3, PDR5, SNQ2, hisl MATa, PDRJ, PDR5, SNQ2, ura3 MATa, pdrl-M::URA3, PDR5, SNQ2 MATa, pdrl-3, PDR5, SNQ2, ura3, hisl, obtained by cross between DRI9-T8 and 2229-5C US50-18C disrupted by pdrl-!J.l::URA3 US50-18C disrupted by pdr5-!J.3::URA3 US50-18C disrupted by snq2::Tn10-LUK US50-D5 disrupted by snq2::Tn10-LUK MATa, PDRJ, PDR5, SNQ2, ade2-2, lysl-1, his4-480, metB-1, SUP4-3 MATa, pdrl-2, PDR5, SNQ2, ade2-2, lysl-1, his4-480, metB-1, SUP4-3 MATa, pdrl-2, PDR5, SNQ2, ura3, his4 US54-17B disrupted by pdrl-!J.l::URA3 MATa, PDRJ, PDR5, SNQ2, adel, hisl MATa, pdrl--S, PDR5, SNQ2, adel, hisl MATa, PDRl, PDR5, SNQ2, leu2, his4, canl-100 MATa, pdrl-7, PDR5, SNQ2, leu2, his4, canl-100 MATa, PDRl, PDR3, PDR5, SNQ2, ura3-52, trpl, leu2-!J.l, his 3-!J.200, GAL2 FY1679-28C disrupted by pdrl-!J.2::TRP1 FY1679-28C disrupted by pdr3-!J.l::HIS3 FY1679-28C/TD disrupted by pdrl-!J.2::TRP1
Summary
Vol 270, No 30, Issue of July 28, pp. 18150-18157, 1995 Printed in U.S.A. Identification and Characterization of SNQ2, a New Multidrug ATP Binding Cassette Transporter of the Yeast Plasma Membrane*. 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 pdrl 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. By selectively deleting or disrupting either the PDR5 or the SNQ2 gene in a pdrl-3 mutant, we were able to distinguish, at the plasma membrane level, the nucleotide triphosphatase activities of the two corresponding proteins independently overexpressed. In a double PDR5,SNQ2 disruptant, the two new ABC transporters PDRll and YOR1 were detected in the overexpressed 160-kDa protein band ofthepdrl-3 mutant.
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