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Gene Review

PDR3  -  Pdr3p

Saccharomyces cerevisiae S288c

Synonyms: AMY2, Pleiotropic drug resistance protein 3, TPE2, Transcription factor PDR3, YBL005W, ...
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High impact information on PDR3

  • Complementation cloning and linkage analysis led to the identification of the dominant mutation TPE1-1 as a new allele of PDR1 and the semidominant mutation tpe2-1 as a new allele of PDR3 [1].
  • These data demonstrated that PDR1 and PDR3 regulate the net rate of M-C6-NBD-PE translocation (flip-flop) and the steady-state distribution of endogenous phosphatidylethanolamine across the plasma membrane [1].
  • The putative consensus Yrr1p binding site deduced from these experiments, (T/A)CCG(C/T)(G/T)(G/T)(A/T)(A/T), is strikingly similar to the PDR element binding site sequence recognized by Pdr1p and Pdr3p [2].
  • Overproduction of PDR3 suppresses mitochondrial import defects associated with a TOM70 null mutation by increasing the expression of TOM72 in Saccharomyces cerevisiae [3].
  • The overproduction of PDR3 mediated this effect by increasing the import of Delta 1,2 pre-F(1)beta into mitochondria [3].

Biological context of PDR3

  • A high-copy-number plasmid carrying the PDR3 gene elevated resistance to both oligomycin and cycloheximide [4].
  • The presence of a functional copy of either PDR1 or PDR3 is essential for drug resistance and expression of a putative membrane transporter-encoding gene, PDR5 [4].
  • Finally, we provide evidence in the absence of PDR1 for a PDR3-controlled transcriptional induction of the drug pump by cycloheximide and propose a model for the mechanism governing the transcriptional autoregulation of Pdr3p [5].
  • The PDR3 gene is positively autoregulated in rho(0) cells by virtue of the presence of two binding sites for Pdr3p in its promoter [6].
  • The resistant phenotype in these groups was found to be caused by allelic forms of the genes AFG2, PDR1, and PDR3 [7].

Anatomical context of PDR3

  • These results indicate that pdr3-1 and pdr3-2 are alleles of the same pleiotropic drug resistance locus PDR3 which is involved in the control of the plasma membrane permeability in yeast [8].
  • The transcription regulators, PDR1 and PDR3, have been shown to activate the transcription of numerous genes involved in a wide range of functions, including resistance to physical and chemical stress, membrane transport, and organelle function in Saccharomyces cerevisiae [1].
  • These data suggest that Pdr1p and Pdr3p may act to modulate the lipid composition of membranes in S. cerevisiae through activation of sphingolipid biosynthesis along with other target genes [9].

Associations of PDR3 with chemical compounds


Physical interactions of PDR3

  • Finally, DNA footprint analysis revealed that the SNQ2 promoter contains three binding sites for Pdr3 [15].
  • An overlapping region of the related transcriptional activator PDR3p was also found to interact with NGG1p [16].
  • Multiple Pdr1p/Pdr3p binding sites are essential for normal expression of the ATP binding cassette transporter protein-encoding gene PDR5 [17].

Regulatory relationships of PDR3

  • Indeed, PDR3 deletion severely reduces benomyl-induced activation of FLR1 gene expression (by 85%), while the homologous Pdr1p transcription factor is apparently not involved in this activation [14].
  • Interestingly, rho(0) strains lacking Lge1p failed to induce PDR3 transcription, but induction was still seen in Deltarad6, Deltabre1, and H2B-K123R mutant strains [6].
  • These pleiotropic drug resistance loci are under the control of the key transcription factors Pdr1p and Pdr3p [18].
  • Pdr3p is involved in a retrograde response in which mitochondrial dysfunctions activate PDR5, a gene encoding an ABC membrane transporter [19].

Other interactions of PDR3

  • Expression of these genes is under the control of two homologous zinc finger-containing transcription regulators, Pdr1p and Pdr3p [20].
  • Transcriptional control of the yeast PDR5 gene by the PDR3 gene product [4].
  • Conversely, HXT11 overexpression increases sensitivity to these drugs in the wild-type strain, an effect which is more pronounced in a strain having both PDR1 and PDR3 deleted [20].
  • The screening is based on the ability to abrogate the growth defect of cells suffering from the galactose induced Pdr3p driven over-expression of a dominant-lethal allele of the PMA1 gene placed under the control of the PDR5 promoter [21].
  • We show that HSF activates expression of PDR3, encoding a multidrug resistance (MDR) transcription factor that also directly activates RPN4 gene expression [22].

Analytical, diagnostic and therapeutic context of PDR3


  1. Plasma membrane translocation of fluorescent-labeled phosphatidylethanolamine is controlled by transcription regulators, PDR1 and PDR3. Kean, L.S., Grant, A.M., Angeletti, C., Mahé, Y., Kuchler, K., Fuller, R.S., Nichols, J.W. J. Cell Biol. (1997) [Pubmed]
  2. New insights into the pleiotropic drug resistance network from genome-wide characterization of the YRR1 transcription factor regulation system. Le Crom, S., Devaux, F., Marc, P., Zhang, X., Moye-Rowley, W.S., Jacq, C. Mol. Cell. Biol. (2002) [Pubmed]
  3. Overproduction of PDR3 suppresses mitochondrial import defects associated with a TOM70 null mutation by increasing the expression of TOM72 in Saccharomyces cerevisiae. Koh, J.Y., Hájek, P., Bedwell, D.M. Mol. Cell. Biol. (2001) [Pubmed]
  4. Transcriptional control of the yeast PDR5 gene by the PDR3 gene product. Katzmann, D.J., Burnett, P.E., Golin, J., Mahé, Y., Moye-Rowley, W.S. Mol. Cell. Biol. (1994) [Pubmed]
  5. Positive autoregulation of the yeast transcription factor Pdr3p, which is involved in control of drug resistance. Delahodde, A., Delaveau, T., Jacq, C. Mol. Cell. Biol. (1995) [Pubmed]
  6. Transcriptional regulation by Lge1p requires a function independent of its role in histone H2B ubiquitination. Zhang, X., Kolaczkowska, A., Devaux, F., Panwar, S.L., Hallstrom, T.C., Jacq, C., Moye-Rowley, W.S. J. Biol. Chem. (2005) [Pubmed]
  7. Diazaborine resistance in the yeast Saccharomyces cerevisiae reveals a link between YAP1 and the pleiotropic drug resistance genes PDR1 and PDR3. Wendler, F., Bergler, H., Prutej, K., Jungwirth, H., Zisser, G., Kuchler, K., Högenauer, G. J. Biol. Chem. (1997) [Pubmed]
  8. Genetic mapping of nuclear mucidin resistance mutations in Saccharomyces cerevisiae. A new pdr locus on chromosome II. Subik, J., Ulaszewski, S., Goffeau, A. Curr. Genet. (1986) [Pubmed]
  9. Coordinate control of sphingolipid biosynthesis and multidrug resistance in Saccharomyces cerevisiae. Hallstrom, T.C., Lambert, L., Schorling, S., Balzi, E., Goffeau, A., Moye-Rowley, W.S. J. Biol. Chem. (2001) [Pubmed]
  10. Expression regulation of the yeast PDR5 ATP-binding cassette (ABC) transporter suggests a role in cellular detoxification during the exponential growth phase. Mamnun, Y.M., Schüller, C., Kuchler, K. FEBS Lett. (2004) [Pubmed]
  11. Isolation and molecular characterization of the carboxy-terminal pdr3 mutants in Saccharomyces cerevisiae. Simonics, T., Kozovska, Z., Michalkova-Papajova, D., Delahodde, A., Jacq, C., Subik, J. Curr. Genet. (2000) [Pubmed]
  12. Identification and characterization of SNQ2, a new multidrug ATP binding cassette transporter of the yeast plasma membrane. Decottignies, A., Lambert, L., Catty, P., Degand, H., Epping, E.A., Moye-Rowley, W.S., Balzi, E., Goffeau, A. J. Biol. Chem. (1995) [Pubmed]
  13. Different missense mutations in PDR1 and PDR3 genes from clotrimazole-resistant sake yeast are responsible for pleiotropic drug resistance and improved fermentative activity. Mizoguchi, H., Yamauchi, T., Watanabe, M., Yamanaka, H., Nishimura, A., Hanamoto, H. J. Biosci. Bioeng. (2002) [Pubmed]
  14. FLR1 gene (ORF YBR008c) is required for benomyl and methotrexate resistance in Saccharomyces cerevisiae and its benomyl-induced expression is dependent on pdr3 transcriptional regulator. Brôco, N., Tenreiro, S., Viegas, C.A., Sá-Correia, I. Yeast (1999) [Pubmed]
  15. The ATP-binding cassette multidrug transporter Snq2 of Saccharomyces cerevisiae: a novel target for the transcription factors Pdr1 and Pdr3. Mahé, Y., Parle-McDermott, A., Nourani, A., Delahodde, A., Lamprecht, A., Kuchler, K. Mol. Microbiol. (1996) [Pubmed]
  16. Transcriptional activation by yeast PDR1p is inhibited by its association with NGG1p/ADA3p. Martens, J.A., Genereaux, J., Saleh, A., Brandl, C.J. J. Biol. Chem. (1996) [Pubmed]
  17. Multiple Pdr1p/Pdr3p binding sites are essential for normal expression of the ATP binding cassette transporter protein-encoding gene PDR5. Katzmann, D.J., Hallstrom, T.C., Mahé, Y., Moye-Rowley, W.S. J. Biol. Chem. (1996) [Pubmed]
  18. Functional dissection of Pdr1p, a regulator of multidrug resistance in Saccharomyces cerevisiae. Kolaczkowska, A., Kolaczkowski, M., Delahodde, A., Goffeau, A. Mol. Genet. Genomics (2002) [Pubmed]
  19. Genome-wide studies on the nuclear PDR3-controlled response to mitochondrial dysfunction in yeast. Devaux, F., Carvajal, E., Moye-Rowley, S., Jacq, C. FEBS Lett. (2002) [Pubmed]
  20. Multiple-drug-resistance phenomenon in the yeast Saccharomyces cerevisiae: involvement of two hexose transporters. Nourani, A., Wesolowski-Louvel, M., Delaveau, T., Jacq, C., Delahodde, A. Mol. Cell. Biol. (1997) [Pubmed]
  21. Screening for effectors that modify multidrug resistance in yeast. Kozovská, Z., Subik, J. Int. J. Antimicrob. Agents (2003) [Pubmed]
  22. A stress regulatory network for co-ordinated activation of proteasome expression mediated by yeast heat shock transcription factor. Hahn, J.S., Neef, D.W., Thiele, D.J. Mol. Microbiol. (2006) [Pubmed]
  23. Expression of cDNAs encoding barley alpha-amylase 1 and 2 in yeast and characterization of the secreted proteins. Søgaard, M., Svensson, B. Gene (1990) [Pubmed]
  24. Genome microarray analysis of transcriptional activation in multidrug resistance yeast mutants. DeRisi, J., van den Hazel, B., Marc, P., Balzi, E., Brown, P., Jacq, C., Goffeau, A. FEBS Lett. (2000) [Pubmed]
  25. Biased mutagenesis in the N-terminal region by degenerate oligonucleotide gene shuffling enhances secretory expression of barley alpha-amylase 2 in yeast. Fukuda, K., Jensen, M.H., Haser, R., Aghajari, N., Svensson, B. Protein Eng. Des. Sel. (2005) [Pubmed]
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