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Adh  -  Alcohol dehydrogenase

Drosophila melanogaster

 
 
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Disease relevance of Adh

 

High impact information on Adh

  • Using truncated Adh constructs, a nontranscribed segment in the Adh regulatory region was found to be one of the sequences required for homology recognition [6].
  • Polycomb and polyhomeotic proteins are bound to the chromatin at the sites of the repressed w-Adh transgenes [7].
  • In addition, multiple transgenes reduce endogenous Adh transcripts, a result that is strongly analogous to "cosuppression" phenomena described in many plant species but which has not been previously observed in animals [7].
  • When two to six copies of a white promoter-Alcohol dehydrogenase (Adh) reporter fusion gene are introduced into the genome, the expression is progressively reduced both in larvae and adults rather than the expected gene dosage effect [7].
  • TAFs and TFIIA mediate differential utilization of the tandem Adh promoters [8].
 

Chemical compound and disease context of Adh

 

Biological context of Adh

 

Anatomical context of Adh

  • The identification involved hybridization selection of ADH-mRNA and in vitro translation, in situ hybridization to the Adh locus on salivary gland polytene chromosomes and DNA sequencing [2].
  • The mRNA for alcohol dehydrogenase (ADH) in D. melanogaster has been identified by translation in a cell-free system [2].
  • We present evidence that the Drosophila ADH is phylogenetically more closely related to P6, another highly expressed protein from the fat body of Drosophila, than it is to the short-chain dehydrogenases [16].
  • Both early and late Drosophila chorion gene promoters confer correct temporal, tissue and sex specificity on a reporter Adh gene [17].
  • To further examine the proposed structure, site-directed mutations were generated in vitro in a cloned D. melanogaster Adh gene, and the mutant constructs were introduced into the Drosophila germ line through P-element mediated transformation [18].
 

Associations of Adh with chemical compounds

  • From the molecular weight of the mutant protein, and from the known sequence of the ADH gene (Benyajati et al., Proc.Natl.Acad.Sci. USA 78, 2717-2721, 1981), we conclude that the tryptophan codon UGG in position 234 has been changed into a UGA nonsense codon in the CyOnB mutant [19].
  • Analysis of the ADH protein showed an amino acid change from valine to threonine in the active site at position 189 which is also found in D. funebris but is otherwise unique among DROSOPHILA: This difference alone may be responsible for the very low ADH activity found in this species and may cause a difference in substrate usage pattern [20].
  • Furthermore, the cysteine mutant and arginine mutant have different substrate specificity and behave differently on competitive inhibition than wild-type ADH [21].
  • Drosophila melanogaster alcohol dehydrogenase is an example of convergent evolution: it is not related to the ADHs of other organisms, but to short-chain dehydrogenases, which until now have been found only in bacteria and in mammalian steroid hormone metabolism [16].
  • The evolution of the P6-ADH family of proteins is characterized by a dramatic increase in the methionine content of P6 [16].
 

Physical interactions of Adh

 

Regulatory relationships of Adh

  • Here, we provide evidence that this Adh promoter switch is regulated by a zinc finger repressor protein (AEF-1) that is expressed predominantly in adult flies and targets the initiator region of the proximal promoter [26].
  • Purified recombinant Adf-1 expressed in Escherichia coli binds specifically to Adf-1 recognition sites and activates transcription of a synthetic Adh promoter in vitro in a manner indistinguishable from the protein purified from Drosophila [27].
  • In contrast, over expression of FTZ-F1 specifically activates distal Adh expression [25].
  • The genetics of a small autosomal region of Drosophila melanogaster containing the structural gene for alcohol dehydrogenase. VI. Induced revertants of scutoid [28].
 

Other interactions of Adh

 

Analytical, diagnostic and therapeutic context of Adh

References

  1. Alcohol dehydrogenase gene of Drosophila melanogaster: relationship of intervening sequences to functional domains in the protein. Benyajati, C., Place, A.R., Powers, D.A., Sofer, W. Proc. Natl. Acad. Sci. U.S.A. (1981) [Pubmed]
  2. Alcohol dehydrogenase in Drosophila: isolation and characterization of messenger RNA and cDNA clone. Benyajati, C., Wang, N., Reddy, A., Weinberg, E., Sofer, W. Nucleic Acids Res. (1980) [Pubmed]
  3. Polymorphism at the Adh and alpha Gpdh loci in Drosophila melanogaster: effects of rearing temperature on developmental rate, body weight, and some biochemical parameters. Oudman, L., Van Delden, W., Kamping, A., Bijlsma, R. Heredity (1991) [Pubmed]
  4. Alcohol and polyol dehydrogenases are both divided into two protein types, and structural properties cross-relate the different enzyme activities within each type. Jörnvall, H., Persson, M., Jeffery, J. Proc. Natl. Acad. Sci. U.S.A. (1981) [Pubmed]
  5. Enoyl-acyl-carrier-protein reductase and Mycobacterium tuberculosis InhA do not conserve the Tyr-Xaa-Xaa-Xaa-Lys motif in mammalian 11 beta- and 17 beta-hydroxysteroid dehydrogenases and Drosophila alcohol dehydrogenase. Baker, M.E. Biochem. J. (1995) [Pubmed]
  6. Cosuppression of nonhomologous transgenes in Drosophila involves mutually related endogenous sequences. Pal-Bhadra, M., Bhadra, U., Birchler, J.A. Cell (1999) [Pubmed]
  7. Cosuppression in Drosophila: gene silencing of Alcohol dehydrogenase by white-Adh transgenes is Polycomb dependent. Pal-Bhadra, M., Bhadra, U., Birchler, J.A. Cell (1997) [Pubmed]
  8. TAFs and TFIIA mediate differential utilization of the tandem Adh promoters. Hansen, S.K., Tjian, R. Cell (1995) [Pubmed]
  9. Effects of differential alcohol dehydrogenase activity on the developmental toxicity of ethanol in Drosophila melanogaster. Ranganathan, S., Davis, D.G., Leeper, J.D., Hood, R.D. Teratology (1987) [Pubmed]
  10. Acetaldehyde utilization and toxicity in Drosophila adults lacking alcohol dehydrogenase or aldehyde oxidase. David, J.R., Daly, K., Van Herrewege, J. Biochem. Genet. (1984) [Pubmed]
  11. Teratogenicity and toxicity of ethylene glycol monomethyl ether (2-methoxyethanol) in Drosophila melanogaster: involvement of alcohol dehydrogenase activity. Eisses, K.T. Teratog., Carcinog. Mutagen. (1989) [Pubmed]
  12. Molecular analysis of the Adh region of the genome of Drosophila melanogaster. Chia, W., Karp, R., McGill, S., Ashburner, M. J. Mol. Biol. (1985) [Pubmed]
  13. The genetics of a small autosomal region of Drosophila melanogaster containing the structural gene for alcohol dehydrogenase. I. Characterization of deficiencies and mapping of ADH and visible mutations. Woodruff, R.C., Ashburner, M. Genetics (1979) [Pubmed]
  14. Protein variation in Adh and Adh-related in Drosophila pseudoobscura. Linkage disequilibrium between single nucleotide polymorphisms and protein alleles. Schaeffer, S.W., Walthour, C.S., Toleno, D.M., Olek, A.T., Miller, E.L. Genetics (2001) [Pubmed]
  15. Partial Characterization and Evolution of Adh-Adhr in Drosophila dunni. Colón-Parrilla, W.V., Pérez-Chiesa, I. Biochem. Genet. (2007) [Pubmed]
  16. Drosophila fat body protein P6 and alcohol dehydrogenase are derived from a common ancestral protein. Rat, L., Veuille, M., Lepesant, J.A. J. Mol. Evol. (1991) [Pubmed]
  17. Both early and late Drosophila chorion gene promoters confer correct temporal, tissue and sex specificity on a reporter Adh gene. Romano, C.P., Bienz-Tadmor, B., Mariani, B.D., Kafatos, F.C. EMBO J. (1988) [Pubmed]
  18. Site-directed mutations reveal long-range compensatory interactions in the Adh gene of Drosophila melanogaster. Parsch, J., Tanda, S., Stephan, W. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  19. In vitro suppression of a nonsense mutant of Drosophila melanogaster. Kubli, E., Schmidt, T., Martin, P.F., Sofer, W. Nucleic Acids Res. (1982) [Pubmed]
  20. Isolation and characterization of the genomic region from Drosophila kuntzei containing the Adh and Adhr genes. Oppentocht, J.E., van Delden, W., van de Zande, L. Mol. Biol. Evol. (2002) [Pubmed]
  21. Site-specific mutagenesis of Drosophila alcohol dehydrogenase: evidence for involvement of tyrosine-152 and lysine-156 in catalysis. Chen, Z., Jiang, J.C., Lin, Z.G., Lee, W.R., Baker, M.E., Chang, S.H. Biochemistry (1993) [Pubmed]
  22. A Drosophila CREB/ATF transcriptional activator binds to both fat body- and liver-specific regulatory elements. Abel, T., Bhatt, R., Maniatis, T. Genes Dev. (1992) [Pubmed]
  23. Drosophila transcriptional repressor protein that binds specifically to negative control elements in fat body enhancers. Falb, D., Maniatis, T. Mol. Cell. Biol. (1992) [Pubmed]
  24. A Drosophila GATA family member that binds to Adh regulatory sequences is expressed in the developing fat body. Abel, T., Michelson, A.M., Maniatis, T. Development (1993) [Pubmed]
  25. Activation and repression of Drosophila alcohol dehydrogenase distal transcription by two steroid hormone receptor superfamily members binding to a common response element. Ayer, S., Walker, N., Mosammaparast, M., Nelson, J.P., Shilo, B.Z., Benyajati, C. Nucleic Acids Res. (1993) [Pubmed]
  26. Regulation of Drosophila Adh promoter switching by an initiator-targeted repression mechanism. Ren, B., Maniatis, T. EMBO J. (1998) [Pubmed]
  27. Cloning of Drosophila transcription factor Adf-1 reveals homology to Myb oncoproteins. England, B.P., Admon, A., Tjian, R. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  28. The genetics of a small autosomal region of Drosophila melanogaster containing the structural gene for alcohol dehydrogenase. VI. Induced revertants of scutoid. Ashburner, M., Detwiler, C., Tsubota, S., Woodruff, R.C. Genetics (1983) [Pubmed]
  29. Climatic selection on genes and traits after a 100 year-old invasion: a critical look at the temperate-tropical clines in Drosophila melanogaster from eastern Australia. Hoffmann, A.A., Weeks, A.R. Genetica (2007) [Pubmed]
  30. The genetics of a small chromosome region of Drosophila melanogaster containing the structural gene for alcohol dehydrogenase. IV: scutoid, an antimorphic mutation. Ashburner, M., Tsubota, S., Woodruff, R.C. Genetics (1982) [Pubmed]
  31. Deletion scanning of the regulatory sequences of the Fbp1 gene of Drosophila melanogaster using P transposase-induced deficiencies. Lapie, P., Nasr, F., Lepesant, J.A., Deutsch, J. Genetics (1993) [Pubmed]
  32. Nonfixed duplication containing the Adh gene and a truncated form of the Adhr gene in the Drosophila funebris species group: different modes of evolution of Adh relative to Adhr in Drosophila. Amador, A., Juan, E. Mol. Biol. Evol. (1999) [Pubmed]
  33. Drosophila alcohol dehydrogenase: acetate-enzyme interactions and novel insights into the effects of electrostatics on catalysis. Benach, J., Winberg, J.O., Svendsen, J.S., Atrian, S., Gonzàlez-Duarte, R., Ladenstein, R. J. Mol. Biol. (2005) [Pubmed]
  34. Site-directed mutagenesis of glycine-14 and two "critical" cysteinyl residues in Drosophila alcohol dehydrogenase. Chen, Z., Lu, L., Shirley, M., Lee, W.R., Chang, S.H. Biochemistry (1990) [Pubmed]
  35. Protein engineering of Drosophila alcohol dehydrogenase. The hydroxyl group of Tyr152 is involved in the active site of the enzyme. Albalat, R., González-Duarte, n.u.l.l., Atrian, S. FEBS Lett. (1992) [Pubmed]
 
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