Skip to main content
Log in

Three alcohol dehydrogenase genes in wild and cultivated barley: Characterization of the products of variant alleles

  • Published:
Biochemical Genetics Aims and scope Submit manuscript

Abstract

Barley (Hordeum vulgare) and its wild progenitor (H. spontaneum) have three loci for alcohol dehydrogenase (EC 1.1.1.1; ADH). The Adh1 locus is constitutively expressed in seed tissues, whereas expression of the loci Adh2 and Adh3 requires anaerobic induction. The Adh3 gene is well expressed in aleurone and embryo tissues kept under N2 for 2–3 days. Using N2-treated embryos, a diverse collection of H. spontaneum was screened in starch gels for electrophoretic variants at the Adh3 locus. Four variants were found: two were conventional mobility variants (Adh3 S, Adh3 V); one was a null variant (Adh3 n); and the fourth (Adh3 I) variant lacked active homodimers and showed reduced heterodimer activity. The 35S-labeled monomers induced under N2 in the lines homozygous for Adh1, Adh2, or Adh3 variants were immunoprecipitated with antiserum raised against maize ADH. Fluorography after separation by SDS-PAGE and by urea-isoelectric focusing indicated that the Adh3 n allele was CRM- and that the Adh3 I gene product was smaller than normal. The Adh1 and Adh3 variants showed independent segregation.

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

  • Banuett-Bourrillon, F., and Hague, D. R. (1979). Genetic analysis of alcohol dehydrogenase isozymes in pearl millet (Pennisetum typhoides). Biochem. Genet. 17537.

    Google Scholar 

  • Banuett-Bourrillon, F. (1982). Linkage of the alcohol dehydrogenase structural genes in pearl millett (Pennisetum typhoides). Biochem. Genet. 20359.

    Google Scholar 

  • Bonner, W. M., and Laskey, R. A. (1974). A film detection method for tritium-labelled proteins and nucleic acids in polyacrylamide gels. Eur. J. Biochem. 4683.

    Google Scholar 

  • Brown, A. H. D. (1980). Genetic basis of alcohol dehydrogenase polymorphism in Hordeum spontaneum. J. Hered 70127.

    Google Scholar 

  • Brown, A. H. D. (1983). Barley. In Tanksley, S. D., and Orton, T. J. (eds.), Isozymes in Plant Genetics and Breeding Elsevier, Amsterdam/New York, Part B. pp. 57–77.

    Google Scholar 

  • Brown, A. H. D., and Jacobsen, J. V. (1982). Genetic basis and natural variation of α-amylase isozymes in barley. Genet. Res. Camb. 40315.

    Google Scholar 

  • Brown, A. H. D., and Munday, J. (1982). Population-genetic structure and optimal sampling of land races of barley from Iran. Genetica 5885.

    Google Scholar 

  • Brown, A. H. D., Nevo, E., Zohary, D., and Dagan, O. (1978). Genetic variation in natural populations of wild barley (Hordeum spontaneum). Genetica 4997.

    Google Scholar 

  • Clegg, M. T., Brown, A. H. D., and Whitfeld, P. R. (1983). Chloroplast DNA diversity of wild and cultivated barley. Genet. Res. (in press).

  • Doll, H., and Brown, A. H. D. (1979). Hordein variation in wild (Hordeum spontaneum) and cultivated (H. vulgare) barley. Can. J. Genet. Cytol. 21391.

    Google Scholar 

  • Ellstrand, N. C., Lee, J. M., and Foster, K. W. (1983). Alcohol dehydrogenase isozymes in grain sorghum (Sorghum bicolor): Evidence of a gene duplication. Biochem. Genet. 21147.

    Google Scholar 

  • Freeling, M., and Birchler, J. A. (1981). Mutants and variants of the alcohol dehydrogenase-1 gene in maize. In Setlow, J. K., and Hollaender, A. (eds.), Genetic Engineering, Principles and Methods Plenum Press, New York, Vol. 3, pp. 223–264.

    Google Scholar 

  • Gerlach, W. L., Pryor, A. J., Dennis, E. S., Ferl, R. J., Sachs, M. M., and Peacock, W. J. (1982). cDNA cloning and induction of the alcohol dehydrogenase gene (Adhl) of mazie. Proc. Natl. Acad. Sci. USA 792981.

    Google Scholar 

  • Hanson, A. D., and Jacobsen, J. V. (1984). Regulated expression of three alcohol dehydrogenase genes in barley aleurone layers. Plant Physiol. (in press).

  • Harberd, N. P., and Edwards, K. J. R. (1982). A mutational analysis of the alcohol dehydrogenase system in barley. Heredity 48187.

    Google Scholar 

  • Harberd, N. P., and Edwards, K. J. R. (1983). Further studies on the alcohol dehydrogenases in barley: Evidence for a third alcohol dehydrogenase locus and data on the effect of an alcohol dehydrogenase-1 mutation in homozygous and in heterozygous condition. Genet. Res. Camb. 41109.

    Google Scholar 

  • Hart, G. E., Islam, A. K. M. R., and Shepherd, K. W. (1980). Use of isozymes as chromosome markers in the isolation and characterization of wheat-barley chromosome addition lines. Genet. Res. Camb. 36311.

    Google Scholar 

  • Islam, A. K. M. R., Shepherd, K. W., and Sparrow, D. H. B. (1981). Isolation and characterization of euplasmic wheat-barley chromosome addition lines. Heredity 46161.

    Google Scholar 

  • Mayne, R. G. (1982). Ph.D. thesis, University of London, London.

    Google Scholar 

  • Nevo, E., Zohary, D., Brown, A. H. D., and Haber, M. (1979). Genetic diversity and environmental associations of wild barley, Hordeum spontaneum, in Israel. Evolution 33815.

    Google Scholar 

  • Okimoto, R., Sachs, M. M., Porter, E. K., and Freeling, M. (1980). Patterns of polypeptide synthesis in various maize organs under anaerobiosis. Planta 15089.

    Google Scholar 

  • Peacock, W. J., Dennis, E. S., Gerlach, W. L., Llewellyn, D., Lörz, H., Pryor, A. J., Sachs, M. M., Schwartz, D., and Sutton, W. D. (1983). Gene transfer in maize: Controlling elements and the alcohol dehydrogenase genes. Miami Winter Symposium (in press).

  • Pryor, A. J., and Huppatz, J. L. (1983). Purification of maize alcohol dehydrogenase and competitive inhibition by pyrazoles. J. Biochem. Intl. 4431.

    Google Scholar 

  • Sachs, M. M., Freeling, M., and Okimoto, R. (1980). The anaerobic proteins of maize. Cell 20761.

    Google Scholar 

  • Spencer, D., Higgins, T. J. V., Button, S. C., and Davey, R. A. (1980). Pulse-labeling studies on protein synthesis in developing pea seeds and evidence of a precursor form of legumin small subunit. Plant Physiol. 66510.

    Google Scholar 

  • Tanksley, S. D., and Jones, R. A. (1981). Effect of O2 stress on tomato alcohol dehydrogenase activity: Description of a second ADH coding gene. Biochem. Genet. 19397.

    Google Scholar 

  • Turner, G. L., and Gibson, A. H. (1980). Measurement of nitrogen fixation by indirect means. In Bergersen, F. J. (ed.), Methods for Evaluating Biological Nitrogen Fixation John Wiley, New York, pp. 111–138.

    Google Scholar 

  • Wignarajah, K., Greenway, H., and John, C. D. (1976). Effect of waterlogging on growth and activity of alcohol dehydrogenase in barley and rice. New Physiol. 77585.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Hanson, A.D., Brown, A.H.D. Three alcohol dehydrogenase genes in wild and cultivated barley: Characterization of the products of variant alleles. Biochem Genet 22, 495–515 (1984). https://doi.org/10.1007/BF00484519

Download citation

  • Received:

  • Revised:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00484519

Key words

Navigation