Display options
Cite
Sealy-Lewis HM, Lockington RA. Regulation of two alcohol dehydrogenases in Aspergillus nidulans. Curr Genet. 1984;8(4):253-9doi: 10.1007/BF00419721.
Sealy-Lewis, H. M., & Lockington, R. A. (1984). Regulation of two alcohol dehydrogenases in Aspergillus nidulans. Current genetics, 8(4), 253-9. https://doi.org/10.1007/BF00419721
Sealy-Lewis, H M, and Lockington, R A. "Regulation of two alcohol dehydrogenases in Aspergillus nidulans." Current genetics vol. 8,4 (1984): 253-9. doi: https://doi.org/10.1007/BF00419721
Sealy-Lewis HM, Lockington RA. Regulation of two alcohol dehydrogenases in Aspergillus nidulans. Curr Genet. 1984 May;8(4):253-9. doi: 10.1007/BF00419721. PMID: 24177792.
Copy Download .nbib Format: NLM
Share it on

Curr Genet. 1984 May;8(4):253-9. doi: 10.1007/BF00419721.

Regulation of two alcohol dehydrogenases in Aspergillus nidulans.

Current genetics

H M Sealy-Lewis, R A Lockington

Affiliations

  1. Department of Biology, University of Essex, Wivenhoe Park, Colchester, C03 3SQ, Essex, England.

PMID: 24177792 DOI: 10.1007/BF00419721

Abstract

In Aspergillus nidulans there are two alcohol dehydrogenases. In the presence of ethanol, alcohol dehydrogenase I (AHH I) is induced and alcohol dehydrogenase II (ADH II) is repressed. ADH I and ADH II have molecular weights of 39,000 and 36,000 respectively. At least ADH I is under the control of alcR, a transacting regulatory gene that is adjacent to alcA (the structural gene for ADH I, Pateman et al. 1983). Mutations in the alcR regulatory gene result in non inducibility of ADH I specific mRNA. Extreme alcA and alcR mutations result in derepressed levels of ADH II, and it is not clear whether alcR controls ADH II directly or through its control of ADH I synthesis. Both enzymes are subject to carbon catabolite repression. Induction of ADH I and ADH II operates at the level of synthesis or processing of mRNA.

References

  1. J Biol Chem. 1977 Nov 25;252(22):8310-9 - PubMed
  2. Nature. 1970 Aug 15;227(5259):680-5 - PubMed
  3. J Immunol. 1975 Dec;115(6):1617-24 - PubMed
  4. Biochim Biophys Acta. 1966 Jan 11;113(1):51-6 - PubMed
  5. Proc Natl Acad Sci U S A. 1976 Feb;73(2):582-4 - PubMed
  6. J Biol Chem. 1982 Mar 25;257(6):3018-25 - PubMed
  7. Proc Natl Acad Sci U S A. 1981 May;78(5):2717-21 - PubMed
  8. Anal Biochem. 1978 Jul 1;87(2):562-5 - PubMed
  9. Methods Enzymol. 1983;96:50-74 - PubMed
  10. Nature. 1980 Jan 10;283(5743):214-6 - PubMed
  11. Mol Gen Genet. 1979;177(1):57-64 - PubMed
  12. Nature. 1982 Dec 23;300(5894):724-8 - PubMed
  13. Proc Natl Acad Sci U S A. 1977 Oct;74(10):4378-81 - PubMed
  14. Mol Gen Genet. 1975;138(2):157-64 - PubMed
  15. Eur J Biochem. 1973 Jul 16;36(2):428-45 - PubMed
  16. Arch Biochem Biophys. 1968 Sep 10;126(3):933-44 - PubMed
  17. Genet Res. 1965 Nov;6(3):352-9 - PubMed
  18. Proc R Soc Lond B Biol Sci. 1983 Feb 22;217(1208):243-64 - PubMed
  19. J Biol Chem. 1983 Feb 25;258(4):2674-82 - PubMed
  20. Eur J Biochem. 1974 Jul 1;46(1):83-8 - PubMed
  21. Cell. 1981 Feb;23(2):605-14 - PubMed
  22. Cell. 1979 Jan;16(1):33-42 - PubMed
  23. Biochem Genet. 1978 Apr;16(3-4):159-70 - PubMed
  24. Mol Gen Genet. 1976 Jun 15;145(3):327-33 - PubMed
  25. Eur J Biochem. 1976 Aug 1;67(1):247-56 - PubMed
  26. Adv Genet. 1953;5:141-238 - PubMed

Publication Types