ArticleScientific reports2019
In vitro NTPase activity of highly purified Pdr5, a major yeast ABC multidrug transporter.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 29 citations in OpenAlex.
- MFS-transporter Flr1 is a major drug-efflux transporter in Saccharomyces cerevisiae ascospores.FEMS yeast research · 2026Article
- An in vitro set-up to study Pdr5-mediated substrate translocation.Protein science : a publication of the Protein Society · 2024Article
- Oligomeric state of the aspartate:alanine transporter from Tetragenococcus halophilus.Journal of biochemistry · 2022Article
- Functional Overexpression of Membrane Proteins in E. coli: The Good, the Bad, and the Ugly.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Structure and efflux mechanism of the yeast pleiotropic drug resistance transporter Pdr5.Nature communications · 2021Article
- Multidrug Resistance in Mammals and Fungi-From MDR to PDR: A Rocky Road from Atomic Structures to Transport Mechanisms.International journal of molecular sciences · 2021Review
- Functional Significance of Conserved Cysteines in the Extracellular Loops of the ATP Binding Cassette Transporter Pdr11p.Journal of fungi (Basel, Switzerland) · 2020Article
- The role of the degenerate nucleotide binding site in type I ABC exporters.FEBS letters · 2020Review
- The first intracellular loop is essential for the catalytic cycle of the human ABCG2 multidrug resistance transporter.FEBS letters · 2020Article
- Review
- Characterization of the nucleotide-binding domain NsrF from the BceAB-type ABC-transporter NsrFP from the human pathogen Streptococcus agalactiae.Scientific reports · 2020Article
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3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The ABC transporter Pdr5 of S. cerevisiae is a key player of the PDR network that works as a first line of defense against a wide range of xenobiotic compounds. As the first discovered member of the family of asymmetric PDR ABC transporters, extensive studies have been carried out to elucidate the molecular mechanism of drug efflux and the details of the catalytic cycle. Pdr5 turned out to be an excellent model system to study functional and structural characteristics of asymmetric, uncoupled ABC transporters. However, to date studies have been limited to in vivo or plasma membrane systems, as it was not possible to isolate Pdr5 in a functional state. Here, we describe the solubilization and purification of Pdr5 to homogeneity in a functional state as confirmed by in vitro assays. The ATPase deficient Pdr5 E1036Q mutant was used as a control and proves that detergent-purified wild-type Pdr5 is functional resembling in its activity the one in its physiological environment. Finally, we show that the isolated active Pdr5 is monomeric in solution. Taken together, our results described in this study will enable a variety of functional investigations on Pdr5 required to determine molecular mechanism of this asymmetric ABC transporter.
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