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Gene Review

ADH1  -  alcohol dehydrogenase ADH1

Saccharomyces cerevisiae S288c

Synonyms: ADC1, Alcohol dehydrogenase 1, Alcohol dehydrogenase I, O0947, YADH-1, ...
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Disease relevance of ADH1


High impact information on ADH1

  • This is consistent with the hypothesis that before the Adh1-Adh2 duplication, yeast did not accumulate ethanol for later consumption but rather used Adh(A) to recycle NADH generated in the glycolytic pathway [5].
  • Yeast later consumes the accumulated ethanol, exploiting Adh2, an Adh1 homolog differing by 24 (of 348) amino acids [5].
  • Pyruvate loses carbon dioxide to produce acetaldehyde, which is reduced by alcohol dehydrogenase 1 (Adh1) to ethanol, which accumulates [5].
  • A similar effect was found at the ADH1 locus, establishing that this effect is not cyc1 gene-specific [6].
  • A yeast strain lacking a functional copy of ADH1 has been isolated that is resistant to antimycin A because of the presence of multiple copies of a nuclear gene, ADH4 [7].

Chemical compound and disease context of ADH1


Biological context of ADH1

  • Expression of some hybrids from the strong ADH1 promoter on multicopy plasmids has a dominant negative effect on silencers, leading to either partial or complete derepression of normally silenced genes [12].
  • Efficient transcription of the glycolytic gene ADH1 and three translational component genes requires the GCR1 product, which can act through TUF/GRF/RAP binding sites [13].
  • The nucleotide sequence of the presumed leader peptide has a high degree of identity with the untranslated leader regions of ADH1 and ADH2 mRNAs [14].
  • Our study also showed that in the large majority of mRNAs, polyadenylation starts directly before or after an adenosine residue and that 3'-end formation of ADH1 transcripts occurs preferentially at the sequence PyAAA [15].
  • The order of these six genes reflects the structure of the ancestral S. cerevisiae genome before the duplication that formed the blocks including ADH1 on chromosome XV and ADH5 on chromosome II, indicating these ADH genes share a direct ancestor [16].

Anatomical context of ADH1


Associations of ADH1 with chemical compounds

  • This enhanced growth was due to a diffusible factor that was shown to be ethanol by chemical assays and evaluation of strains lacking ADH1, ADH3, and ADH5, as all three genes are involved in ethanol production by yeast [22].
  • Ty insertions at two loci account for most of the spontaneous antimycin A resistance mutations during growth at 15 degrees C of Saccharomyces cerevisiae strains lacking ADH1 [23].
  • Furthermore TYE2 function seems to be important for the expression of a variety of Ty-unrelated functions such as ADH1 expression, sporulation, growth on maltose, galactose, raffinose, and on non-fermentable carbon sources [24].
  • Construction of an adh1-0 mutant revealed that yeast lacking a functional ADH1 gene is sensitive to formaldehyde [25].
  • The butanol dehydrogenase gene is referred to as the adh1 gene since it was shown to have activity using butanol and ethanol as substrates [1].

Physical interactions of ADH1


Regulatory relationships of ADH1

  • Reintroduction of a functional PGS1 gene under control of the ADH1 promoter restored phosphatidylglycerol synthesis and expression of mtGFP [27].
  • The expression of ADH1 was activated synergistically by both ABF1 binding sites [28].
  • Chimeric genes that express Itr1p and Itr2p fused to the green fluorescent protein (GFP) under the control of the ADH1 promoter were constructed [29].
  • 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 [30].
  • The coding sequence of the SUC2 locus was placed under the control of the constitutive ADH1 promoter and transcription terminator in a centromere-based yeast plasmid vector from which invertase is expressed in a Suc- strain of Saccharomyces cerevisiae [31].

Other interactions of ADH1

  • Additionally, when the ATM1 3' UTR was replaced by the ADH1 3' UTR, we obtained cells in which ATM1 mRNA is also delocalized, and presenting a respiratory dysfunction [32].
  • The TFIIB mutations conferred downstream shifts in transcription initiation at the ADH1 and CYC1 promoters, whereas no significant shifts were observed at the HIS3 promoter [33].
  • Isolation and DNA sequence of ADH3, a nuclear gene encoding the mitochondrial isozyme of alcohol dehydrogenase in Saccharomyces cerevisiae [14].
  • We have purified extensively the transcriptional activator, GAL4, from a yeast strain overexpressing the gene product from the ADH1 promoter [34].
  • However, in a SUA7+ background, ssu73-1 confers the same upstream shift at ADH1 as an rpb9 null allele [35].

Analytical, diagnostic and therapeutic context of ADH1


  1. Molecular analysis and nucleotide sequence of the adh1 gene encoding an NADPH-dependent butanol dehydrogenase in the Gram-positive anaerobe Clostridium acetobutylicum. Youngleson, J.S., Jones, W.A., Jones, D.T., Woods, D.R. Gene (1989) [Pubmed]
  2. Comparison of expression of the endo-beta-1,3-1,4-glucanase gene from Bacillus subtilis in Saccharomyces cerevisiae from the CYC1 and ADH1 promoters. Cantwell, B.A., Brazil, G., Murphy, N., McConnell, D.J. Curr. Genet. (1986) [Pubmed]
  3. Overexpression, purification and properties of alcohol dehydrogenase IV from Saccharomyces cerevisiae. Drewke, C., Ciriacy, M. Biochim. Biophys. Acta (1988) [Pubmed]
  4. Efficient Production of L-Lactic Acid from Xylose by Pichia stipitis. Ilm??n, M., Koivuranta, K., Ruohonen, L., Suominen, P., Penttil??, M. Appl. Environ. Microbiol. (2007) [Pubmed]
  5. Resurrecting ancestral alcohol dehydrogenases from yeast. Thomson, J.M., Gaucher, E.A., Burgan, M.F., De Kee, D.W., Li, T., Aris, J.P., Benner, S.A. Nat. Genet. (2005) [Pubmed]
  6. The yeast SUA7 gene encodes a homolog of human transcription factor TFIIB and is required for normal start site selection in vivo. Pinto, I., Ware, D.E., Hampsey, M. Cell (1992) [Pubmed]
  7. Resistance to antimycin A in yeast by amplification of ADH4 on a linear, 42 kb palindromic plasmid. Walton, J.D., Paquin, C.E., Kaneko, K., Williamson, V.M. Cell (1986) [Pubmed]
  8. Synthesis of coenzymically active soluble and insoluble macromolecularized NAD+ derivatives. Zappelli, P., Rossodivita, A., Re, L. Eur. J. Biochem. (1975) [Pubmed]
  9. Protection against cadmium toxicity in yeast by alcohol dehydrogenase. Yu, W., Macreadie, I.G., Winge, D.R. J. Inorg. Biochem. (1991) [Pubmed]
  10. Regeneration of intact tobacco plants containing full length copies of genetically engineered T-DNA, and transmission of T-DNA to R1 progeny. Barton, K.A., Binns, A.N., Matzke, A.J., Chilton, M.D. Cell (1983) [Pubmed]
  11. Reduced nicotinamide 8-(alkylamino)adenine dinucleotides: enzyme-coenzyme interactions with different adenyl glycosyl bond conformations. Lappi, D.A., Evans, F.E., Kaplan, N.O. Biochemistry (1980) [Pubmed]
  12. Dissection of a carboxy-terminal region of the yeast regulatory protein RAP1 with effects on both transcriptional activation and silencing. Hardy, C.F., Balderes, D., Shore, D. Mol. Cell. Biol. (1992) [Pubmed]
  13. Efficient transcription of the glycolytic gene ADH1 and three translational component genes requires the GCR1 product, which can act through TUF/GRF/RAP binding sites. Santangelo, G.M., Tornow, J. Mol. Cell. Biol. (1990) [Pubmed]
  14. Isolation and DNA sequence of ADH3, a nuclear gene encoding the mitochondrial isozyme of alcohol dehydrogenase in Saccharomyces cerevisiae. Young, E.T., Pilgrim, D. Mol. Cell. Biol. (1985) [Pubmed]
  15. Identification of pre-mRNA polyadenylation sites in Saccharomyces cerevisiae. Heidmann, S., Obermaier, B., Vogel, K., Domdey, H. Mol. Cell. Biol. (1992) [Pubmed]
  16. Kluyveromyces marxianus exhibits an ancestral Saccharomyces cerevisiae genome organization downstream of ADH2. Ladrière, J.M., Georis, I., Guérineau, M., Vandenhaute, J. Gene (2000) [Pubmed]
  17. Oxygen and carbon source-regulated expression of PDC and ADH genes in the respiratory yeast Pichia anomala. Fredlund, E., Beerlage, C., Melin, P., Schn??rer, J., Passoth, V. Yeast (2006) [Pubmed]
  18. Efficient selection of hybrids by protoplast fusion using drug resistance markers and reporter genes in Saccharomyces cerevisiae. Nakazawa, N., Iwano, K. J. Biosci. Bioeng. (2004) [Pubmed]
  19. Identification of the plasma membrane H+-biotin symporter of Saccharomyces cerevisiae by rescue of a fatty acid-auxotrophic mutant. Stolz, J., Hoja, U., Meier, S., Sauer, N., Schweizer, E. J. Biol. Chem. (1999) [Pubmed]
  20. Ultrastructural analysis of the autophagic process in yeast: detection of autophagosomes and their characterization. Baba, M., Takeshige, K., Baba, N., Ohsumi, Y. J. Cell Biol. (1994) [Pubmed]
  21. Multiple forms of mitochondrial alcohol dehydrogenase in Saccharomyces cerevisiae. Wiesenfeld, M., Schimpfessel, L., Crokaert, R. Biochim. Biophys. Acta (1975) [Pubmed]
  22. Microbial synergy via an ethanol-triggered pathway. Smith, M.G., Des Etages, S.G., Snyder, M. Mol. Cell. Biol. (2004) [Pubmed]
  23. Ty insertions at two loci account for most of the spontaneous antimycin A resistance mutations during growth at 15 degrees C of Saccharomyces cerevisiae strains lacking ADH1. Paquin, C.E., Williamson, V.M. Mol. Cell. Biol. (1986) [Pubmed]
  24. Isolation of the TYE2 gene reveals its identity to SWI3 encoding a general transcription factor in Saccharomyces cerevisiae. Löhning, C., Rosenbaum, C., Ciriacy, M. Curr. Genet. (1993) [Pubmed]
  25. Overexpression of ADH1 confers hyper-resistance to formaldehyde in Saccharomyces cerevisiae. Grey, M., Schmidt, M., Brendel, M. Curr. Genet. (1996) [Pubmed]
  26. Identification of functional regions in the yeast transcriptional activator ADR1. Bemis, L.T., Denis, C.L. Mol. Cell. Biol. (1988) [Pubmed]
  27. Translational regulation of nuclear gene COX4 expression by mitochondrial content of phosphatidylglycerol and cardiolipin in Saccharomyces cerevisiae. Su, X., Dowhan, W. Mol. Cell. Biol. (2006) [Pubmed]
  28. Transcriptional control of the Saccharomyces cerevisiae ADH1 gene by autonomously replicating sequence binding factor 1. Yoo, H.Y., Jung, S.Y., Kim, Y.H., Kim, J., Jung, G., Rho, H.M. Curr. Microbiol. (1995) [Pubmed]
  29. Mutational analysis and localization of the inositol transporters of Saccharomyces cerevisiae. Miyashita, M., Shugyo, M., Nikawa, J. J. Biosci. Bioeng. (2003) [Pubmed]
  30. 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]
  31. Cassette mutagenic analysis of the yeast invertase signal peptide: effects on protein translocation. Ngsee, J.K., Hansen, W., Walter, P., Smith, M. Mol. Cell. Biol. (1989) [Pubmed]
  32. In Saccharomyces cerevisiae, ATP2 mRNA sorting to the vicinity of mitochondria is essential for respiratory function. Margeot, A., Blugeon, C., Sylvestre, J., Vialette, S., Jacq, C., Corral-Debrinski, M. EMBO J. (2002) [Pubmed]
  33. Promoter-specific shifts in transcription initiation conferred by yeast TFIIB mutations are determined by the sequence in the immediate vicinity of the start sites. Faitar, S.L., Brodie, S.A., Ponticelli, A.S. Mol. Cell. Biol. (2001) [Pubmed]
  34. Purification and characterization of the yeast transcriptional activator GAL4. Parthun, M.R., Jaehning, J.A. J. Biol. Chem. (1990) [Pubmed]
  35. Functional interaction between TFIIB and the Rpb9 (Ssu73) subunit of RNA polymerase II in Saccharomyces cerevisiae. Sun, Z.W., Tessmer, A., Hampsey, M. Nucleic Acids Res. (1996) [Pubmed]
  36. Characterization of low-acetic-acid-producing yeast isolated from 2-deoxyglucose-resistant mutants and its application to high-gravity brewing. Mizuno, A., Tabei, H., Iwahuti, M. J. Biosci. Bioeng. (2006) [Pubmed]
  37. RNA polymerase II elongation factors of Saccharomyces cerevisiae: a targeted proteomics approach. Krogan, N.J., Kim, M., Ahn, S.H., Zhong, G., Kobor, M.S., Cagney, G., Emili, A., Shilatifard, A., Buratowski, S., Greenblatt, J.F. Mol. Cell. Biol. (2002) [Pubmed]
  38. Protein engineering of alcohol dehydrogenases: effects of amino acid changes at positions 93 and 48 of yeast ADH1. Creaser, E.H., Murali, C., Britt, K.A. Protein Eng. (1990) [Pubmed]
  39. Pyrene excimer fluorescence of yeast alcohol dehydrogenase: a sensitive probe to investigate ligand binding and unfolding pathway of the enzyme. Santra, M.K., Dasgupta, D., Panda, D. Photochem. Photobiol. (2006) [Pubmed]
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