Skip to main content
Log in

Regulation of two alcohol dehydrogenases in Aspergillus nidulans

  • Original Articles
  • Published:
Current Genetics Aims and scope Submit manuscript

Summary

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.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  • Beier DR, Young ET (1982) Nature 300:724–728

    Google Scholar 

  • Bennetzen JL, Hall BD (1982) Biol Chem 257:3018–3025

    Google Scholar 

  • Benyati C, Place AR, Powers DA, Sofer W (1981) Proc Natl Acad Sci USA 78:2717–2721

    Google Scholar 

  • Bonner WM, Laskey RA (1974) Eur J Biochem 46:83–88

    Google Scholar 

  • Ciriacy M (1975a) Mutat Res 25:315–326

    Google Scholar 

  • Ciriacy M (1975b) Mol Gen Genet 138:157–164

    Google Scholar 

  • Ciriacy M (1976) Mol Gen Genet 145:327–333

    Google Scholar 

  • Cove DJ (1966) Biochem Biophys Acta 113:51–56

    Google Scholar 

  • Cox RA (1978) Methods Enzymol 12B:120–129

    Google Scholar 

  • Deeley RG, Gordon J, Burns AJH, Mullinix KP, Binastein M, Goldberger RF (1977) J Biol Chem 252:8310–8319

    Google Scholar 

  • Dottavia-Martin D, Ravel JM (1978) Anal Biochem 87:562–565

    Google Scholar 

  • Hynes MJ, Corrick CM, King JA (1983) Mol Cellular Biol (In press)

  • Jackson RJ, Hunt T (1983) Methods Enzymol 96:50–74

    Google Scholar 

  • Kessler SW (1975) A J Immunol 115:1617–1624

    Google Scholar 

  • Laemmli UK (1970) Nature 227:680–685

    Google Scholar 

  • Lewis NJ, Gilbert J (1978) Biochem Genet 16:159–170

    Google Scholar 

  • Li Ti-K, Bosron WF, Dateldecker WP, Lange LG, Vallee BL (1977) Proc Natl Acad Sci USA 74:4378–4381

    Google Scholar 

  • Lutstorf U, Megnet R (1968) Arch Biochem Biophys 126:933–944

    Google Scholar 

  • McCully KS, Forbes E (1965) Genet Res 6:352–359

    Google Scholar 

  • McDonald JF, Chambers GKL, David J, Ayala FJ (1977) Proc Natl Acad Sci USA 74:4378–4381

    Google Scholar 

  • Page MM (1971) PhD thesis, University of Cambridge

  • Pateman JA, Doy CH, Olsen JE, Norris U, Creaser EH, Hynes M (1983) Proc R Soc Lond B217:243–264

    Google Scholar 

  • Pelham HRB, Jackson RJ (1976) Eur J Biochem 67:247–256

    Google Scholar 

  • Roberts TJ, Martinelli S, Scazzocchio C (1979) Mol Gen Genet 177:57–64

    Google Scholar 

  • Pontecorvo G, Roper JA, Hemmons LM, MacDonald KD, Bufton AWJ (1953) Adv Genet 5:141–238

    Google Scholar 

  • Russell DW, Smith M, Williamson VM, Young ET (1983) J Biol Chem 258:2674–2682

    Google Scholar 

  • Scazzocchio C, Holl FB, Foguelman AI (1973) Eur J Biochem 36:428–445

    Google Scholar 

  • Schwarz D (1976) Proc Natl Acad Sci USA 73:582–584

    Google Scholar 

  • Smith M, Hopkinson DA, Harris H (1973) Ann Hum Genet 37:1929–1933.

    Google Scholar 

  • Thorley-Lawson DA (1979) Cell 16:33–42

    Google Scholar 

  • Williamson VM, Bennetzen J, Young ET, Nasmyth K, Hall BD (1980) Nature 283:214–216

    Google Scholar 

  • Williamson VM, Young ET, Ciriacy M (1981) Cell 23:605–614

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Sealy-Lewis, H.M., Lockington, R.A. Regulation of two alcohol dehydrogenases in Aspergillus nidulans . Curr Genet 8, 253–259 (1984). https://doi.org/10.1007/BF00419721

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00419721

Key words

Navigation