The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Gene Review

ADR1  -  Adr1p

Saccharomyces cerevisiae S288c

Synonyms: Regulatory protein ADR1, YD8142.16, YD8142B.08, YDR216W
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of ADR1


High impact information on ADR1

  • Our data suggest that glucose repression of ADH2 is in part mediated through a cAMP-dependent phosphorylation-inactivation of the ADR1 regulatory protein [3].
  • Cyclic AMP-dependent protein kinase phosphorylates and inactivates the yeast transcriptional activator ADR1 [3].
  • A structure for a single zinc-finger from the yeast protein ADR1, was recently proposed based on two-dimensional NMR data (ref. 8), and a similar structure was proposed based on comparison with crystal structures of other metalloproteins [4].
  • Only one other mutation caused an adr1 null phenotype [5].
  • Nineteen independently isolated adr1 mutations induced by hydroxylamine were found at nine different amino-acid positions, seven of which are in the two finger domains [5].

Biological context of ADR1


Anatomical context of ADR1


Associations of ADR1 with chemical compounds

  • These microarray data show that ADR1 coordinates the biochemical pathways that generate acetyl-CoA and NADH from non-fermentable substrates [9].
  • Our data suggest that a functional domain of the ADR1 protein localized between residues 643 and 1323 is required for the induction of peroxisomal structures and for the utilization of oleic acid [10].
  • Alanine scanning site-directed mutagenesis of the zinc fingers of transcription factor ADR1: residues that contact DNA and that transactivate [11].
  • This suggests that glucose can block ADR1-mediated activation independently of cAMP-dependent phosphorylation at serine 230 [12].
  • One strain resistant to ADR1-induced petite formation displayed cross-resistance to petite mutation by growth at elevated temperature and euflavine treatment, yet was susceptible to petite induction by ethidium bromide [13].

Physical interactions of ADR1

  • In conclusion, these results show a derepression of ADH2 by synergistically acting regulators Adr1 (interacting with UAS1) and Cat8, binding to UAS2 (=CSRE(ADH2)) [14].
  • By using gene fusions encoding the Gal4p DNA binding domain and portions of Adr1p, we identified a single, strong acidic activation domain spanning amino acids 420-462 of Adr1p [8].
  • UAS(ADR1) is a presumed binding site for the zinc finger transcription factor Adr1p and UAS(INO) is a presumed binding site for the basic helix-loop-helix transcription factors Ino2p and Ino4p [15].
  • The transcriptional activator ADR1 from Saccharomyces cerevisiae is a postulated DNA-binding protein that controls the expression of the glucose-repressible alcohol dehydrogenase (ADH2) [16].
  • ADR1 was found to associate in vivo with TFIID in that immunoprecipitation of either TAFII90 or TBP from yeast whole-cell extracts specifically coimmunoprecipitated ADR1 [17].

Regulatory relationships of ADR1

  • The yeast transcriptional activator Adr1p controls expression of the glucose-repressible alcohol dehydrogenase gene (ADH2), genes involved in glycerol metabolism, and genes required for peroxisome biogenesis and function [8].
  • From this it was concluded that CCR1 specifies for a product co-activating the structural gene or modifying the ADR1-gene product [18].
  • The ability of ADR1 to increase the frequency of mitochondrial mutation is correlated with its ability to activate ADH II transcription but is independent of the level of ADH II being expressed [13].
  • Electrophoretic mobility shift analysis demonstrated that Adr1p bound to UAS1PIP2, and Northern analysis in combination with a lacZ reporter gene confirmed that Adr1p influenced the transcription of PIP2 [19].

Other interactions of ADR1

  • Compared with wild-type cells, adr1 null mutants produced by disruption of the gene exhibit reduced CTA1 expression [7].
  • The yeast transcriptional activator ADR1, which is required for ADH2 and peroxisomal gene expression, contains four separable and partially redundant activation domains (TADs) [20].
  • However, nearly one-half of the ADR1-dependent genes are also dependent on the Snf1 protein kinase for derepression [9].
  • Only a small number of ADR1-dependent genes are also CAT8-dependent [9].
  • The contact to and dependence on GCN5, a histone acetyltransferase, suggests that rearrangement of nucleosomes may be one important means by which ADR1 activates transcription [20].

Analytical, diagnostic and therapeutic context of ADR1


  1. Transcriptional control of the yeast acetyl-CoA synthetase gene, ACS1, by the positive regulators CAT8 and ADR1 and the pleiotropic repressor UME6. Kratzer, S., Schüller, H.J. Mol. Microbiol. (1997) [Pubmed]
  2. DNABIND: an interactive microcomputer program searching for nucleotide sequences that may code for conserved DNA-binding protein motifs. Mrázek, J., Kypr, J. Comput. Appl. Biosci. (1992) [Pubmed]
  3. Cyclic AMP-dependent protein kinase phosphorylates and inactivates the yeast transcriptional activator ADR1. Cherry, J.R., Johnson, T.R., Dollard, C., Shuster, J.R., Denis, C.L. Cell (1989) [Pubmed]
  4. Transcription factor IIIA induced bending of the Xenopus somatic 5S gene promoter. Schroth, G.P., Cook, G.R., Bradbury, E.M., Gottesfeld, J.M. Nature (1989) [Pubmed]
  5. Two zinc fingers of a yeast regulatory protein shown by genetic evidence to be essential for its function. Blumberg, H., Eisen, A., Sledziewski, A., Bader, D., Young, E.T. Nature (1987) [Pubmed]
  6. Sequence homology of the yeast regulatory protein ADR1 with Xenopus transcription factor TFIIIA. Hartshorne, T.A., Blumberg, H., Young, E.T. Nature (1986) [Pubmed]
  7. The Saccharomyces cerevisiae ADR1 gene is a positive regulator of transcription of genes encoding peroxisomal proteins. Simon, M., Adam, G., Rapatz, W., Spevak, W., Ruis, H. Mol. Cell. Biol. (1991) [Pubmed]
  8. Characterization of a p53-related activation domain in Adr1p that is sufficient for ADR1-dependent gene expression. Young, E.T., Saario, J., Kacherovsky, N., Chao, A., Sloan, J.S., Dombek, K.M. J. Biol. Chem. (1998) [Pubmed]
  9. Multiple pathways are co-regulated by the protein kinase Snf1 and the transcription factors Adr1 and Cat8. Young, E.T., Dombek, K.M., Tachibana, C., Ideker, T. J. Biol. Chem. (2003) [Pubmed]
  10. A C-terminal region of the Saccharomyces cerevisiae transcription factor ADR1 plays an important role in the regulation of peroxisome proliferation by fatty acids. Simon, M.M., Pavlik, P., Hartig, A., Binder, M., Ruis, H., Cook, W.J., Denis, C.L., Schanz, B. Mol. Gen. Genet. (1995) [Pubmed]
  11. Alanine scanning site-directed mutagenesis of the zinc fingers of transcription factor ADR1: residues that contact DNA and that transactivate. Thukral, S.K., Morrison, M.L., Young, E.T. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  12. ADH2 expression is repressed by REG1 independently of mutations that alter the phosphorylation of the yeast transcription factor ADR1. Dombek, K.M., Camier, S., Young, E.T. Mol. Cell. Biol. (1993) [Pubmed]
  13. Overexpression of the yeast transcriptional activator ADR1 induces mutation of the mitochondrial genome. Cherry, J.R., Denis, C.L. Curr. Genet. (1989) [Pubmed]
  14. Adr1 and Cat8 synergistically activate the glucose-regulated alcohol dehydrogenase gene ADH2 of the yeast Saccharomyces cerevisiae. Walther, K., Schüller, H.J. Microbiology (Reading, Engl.) (2001) [Pubmed]
  15. Expression of GUT1, which encodes glycerol kinase in Saccharomyces cerevisiae, is controlled by the positive regulators Adr1p, Ino2p and Ino4p and the negative regulator Opi1p in a carbon source-dependent fashion. Grauslund, M., Lopes, J.M., Rønnow, B. Nucleic Acids Res. (1999) [Pubmed]
  16. Identification of functional regions in the yeast transcriptional activator ADR1. Bemis, L.T., Denis, C.L. Mol. Cell. Biol. (1988) [Pubmed]
  17. ADR1-mediated transcriptional activation requires the presence of an intact TFIID complex. Komarnitsky, P.B., Klebanow, E.R., Weil, P.A., Denis, C.L. Mol. Cell. Biol. (1998) [Pubmed]
  18. Isolation and characterization of further cis- and trans-acting regulatory elements involved in the synthesis of glucose-repressible alcohol dehydrogenase (ADHII) in Saccharomyces cerevisiae. Ciriacy, M. Mol. Gen. Genet. (1979) [Pubmed]
  19. Saccharomyces cerevisiae PIP2 mediating oleic acid induction and peroxisome proliferation is regulated by Adr1p and Pip2p-Oaf1p. Rottensteiner, H., Wabnegger, L., Erdmann, R., Hamilton, B., Ruis, H., Hartig, A., Gurvitz, A. J. Biol. Chem. (2003) [Pubmed]
  20. ADR1 activation domains contact the histone acetyltransferase GCN5 and the core transcriptional factor TFIIB. Chiang, Y.C., Komarnitsky, P., Chase, D., Denis, C.L. J. Biol. Chem. (1996) [Pubmed]
  21. Dissection of the ADR1 protein reveals multiple, functionally redundant activation domains interspersed with inhibitory regions: evidence for a repressor binding to the ADR1c region. Cook, W.J., Chase, D., Audino, D.C., Denis, C.L. Mol. Cell. Biol. (1994) [Pubmed]
  22. Isolation and characterization of the positive regulatory gene ADR1 from Saccharomyces cerevisiae. Denis, C.L., Young, E.T. Mol. Cell. Biol. (1983) [Pubmed]
  23. Isoform-specific purification and substrate specificity of the 5'-AMP-activated protein kinase. Michell, B.J., Stapleton, D., Mitchelhill, K.I., House, C.M., Katsis, F., Witters, L.A., Kemp, B.E. J. Biol. Chem. (1996) [Pubmed]
  24. Mechanism of DNA binding by the ADR1 zinc finger transcription factor as determined by SPR. Schaufler, L.E., Klevit, R.E. J. Mol. Biol. (2003) [Pubmed]
  25. Designing zinc-finger ADR1 mutants with altered specificity of DNA binding to T in UAS1 sequences. Taylor, W.E., Suruki, H.K., Lin, A.H., Naraghi-Arani, P., Igarashi, R.Y., Younessian, M., Katkus, P., Vo, N.V. Biochemistry (1995) [Pubmed]
WikiGenes - Universities