Skip to main content
Log in

A Mutant of Arabidopsis thaliana lpar;L.) Heynh. with Modified Control of Aspartate Kinase by Threonine

  • Published:
Biochemical Genetics Aims and scope Submit manuscript

Abstract

Mutagenesis and subsequent selection of Arabidopsis thaliana plantlets on a growth inhibitory concentration of lysine has led to the isolation of lysine-resistant mutants. The ability to grow on 2 m M lysine has been used to isolate mutants that may contain an aspartate kinase with altered regulatory-feedback properties. One of these mutants (RL 4) was characterized by a relative enhancement of soluble lysine. The recessive monogenic nuclear transmission of the resistance trait was established. It was associated with an aspartate kinase less sensitive to feedback inhibition by threonine. Two mutants (RLT 40 and RL 4) in Arabidopsis, characterized by an altered regulation of aspartate kinase, were crossed to assess the effects of the simultaneous presence of these different aspartate kinase forms. A double mutant (RLT40 × RL4) was isolated and characterized by two feedback-desensitized isozymes of aspartate kinase to, respectively, lysine and threonine but no threonine and/or lysine overproduction was observed. Genetical analysis of this unique double aspartate kinase mutant indicated that both mutations were located on chromosome 2, but their loci (ak1and ak2) were found to be unlinked.

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

  • Arruda, P., Bright, S. W. J., Kueh, J. S. H., Lea, P. J., and Rognes, S. E. (1984). Regulation of aspartate kinase isoenzymes in barley mutants resistant to lysine plus threonine. Plant Physiol. 76:442.

    Google Scholar 

  • Azevedo, R. A., Blackwell, R. D., Smith, R. J., and Lea, P. J. (1992). Three aspartate kinase isoenzymes from maize. Phytochemistry 31:3725.

    Google Scholar 

  • Bieleski, R. L., and Turner, N. A. (1966). Separation and estimation of amino acids in crude plant extracts by thin-layer electrophoresis and chromatography. Anal. Biochem. 17:278.

    Google Scholar 

  • Black, S., and Wright, N. G. (1955). Aspartic β-semialdehyde dehydrogenase and aspartic β-semialdehyde. J. Biol. Chem. 213:39.

    Google Scholar 

  • Bradford, M. M. (1976). A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248.

    Google Scholar 

  • Bright, S. W. J., Miflin, B. J., and Rognes, S. E. (1982). Threonine accumulation in the seeds of a barley mutant with an altered aspartate kinase. Biochem. Genet. 20:229.

    Google Scholar 

  • Bryan, J. K. (1980). Synthesis of the aspartate family and the branched-chain amino acids. In Miflin, B. J. (ed.), The Biochemistry of Plants, Vol. 5. Amino Acids and Derivatives, Academic Press, New York, pp. 403–452.

    Google Scholar 

  • Dotson, S. B., Frisch, D. A., Somers, D. A., and Gengenbach, B. G. (1990). Lysine-insensitive aspartate kinase in two threonine-overproducing mutants of maize. Planta 182:546.

    Google Scholar 

  • Frankard, V., Ghislain, M., Negrutiu, I., and Jacobs, M. (1991). High threonine producer mutant of Nicotiana sylvestris (Spegg. and Comes). Theor. Appl. Genet. 82:273.

    Google Scholar 

  • Frisch, D. A., and Gengenbach, B. G. (1986). Allelism test for two threonine-overproducing mutants. Maize Genet. Coop. Newslett. 60:115.

    Google Scholar 

  • Galili, G. (1995). Regulation of lysine and threonine synthesis. Plant Cell 7:899.

    Google Scholar 

  • Hauge, B. M., Hanley, S. M., Cartinhour, S., Cherry, J. M., and Goodman, H. M. (1993). An integrated genetic/RFLP map of the Arabidopsis thaliana genome. Plant J. 3(5):745.

    Google Scholar 

  • Heremans. B., and Jacobs, M. (1994). Selection of Arabidopsis thaliana (L.) Heynh. mutants resistant to aspartate-derived amino acids and analogues. Plant Sci. 101:151.

    Google Scholar 

  • Heremans, B., and Jacobs, M. (1995). Threonine accumulation in a mutant of Arabidopsis thaliana (L.) Heynh. with an altered aspartate kinase. J. Plant Physiol. 101:249.

    Google Scholar 

  • Hibberd, K. A., Green, T. W. C. E., and Gengenbach, B. G. (1980). Selection and characterization of a feedback-insensitive tissue culture of maize. Planta 148:183.

    Google Scholar 

  • Kochhar, S., Kochhar, V. K., and Sane, P. V. (1986). Isolation, characterization and regulation of isoenzymes of aspartate kinase differentially sensitive to calmoduline from spinach leaves. Biochim. Biophys. Acta 880:220.

    Google Scholar 

  • Koornneef, M. (1990). Linkage map of Arabidopsis thaliana (2n = 10). In O'Brien, S. J. (ed.), Genetic Maps, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp 6.95–6.97.

    Google Scholar 

  • Lea, P. J., Mills, W. R., and Miflin, B. J. (1979). The isolation of a lysine-sensitive aspartate kinase from pea leaves and its involvement in homoserine biosynthesis in isolated chloroplasts. FEBS Lett. 98(1):165.

    Google Scholar 

  • Muehlbauer, G. J., Somers, D. A., Matthews, B. F., and Gengenbach, B. G. (1994). Molecular genetics of the maize aspartate kinase-homoserine dehydrogenasegene family (submitted for publication).

  • Oostindiër-Braaksma, F. J., and Feenstra, W. J. (1973). Isolation and characterization of chlorateresistant mutants of Arabidopsis thaliana. Mutat. Res. 19:175.

    Google Scholar 

  • Piryns, I., Vernaillen, S., and Jacobs, M. (1988). Inhibitory effects of aspartate-derived amino acids and aminoethylcysteine, a lysine analog, on the growth of sorghum seedlings; relation with three enzymes of the aspartate-pathway. Plant Sci. 57:93.

    Google Scholar 

  • Rognes, S. E., Bright, S. W. J., and Miflin, B. J. (1983). Feedback-insensitive aspartate kinase isoenzymes in barley mutants resistant to lysine plus threonine. Planta 157:32.

    Google Scholar 

  • Serra, J. A. (1965). Cross-over values and recombination maps. In Serra, J. A. (ed.), Modern Genetics, Vol. 3, Academic Press, London, p. 249.

    Google Scholar 

  • Wilson, B. J., Gray, A. C., and Matthews, B. F. (1991). Bifunctional protein in carrot contains both aspartokinase and homoserine dehydrogenase activities. Plant Physiol. 97:1323.

    Google Scholar 

  • Wong, K. F., and Dennis, D. T. (1973a). Aspartokinase from wheat germ. Isolation, characterization and regulation. Plant Physiol. 51:322.

    Google Scholar 

  • Wong, K. F., and Dennis, D. T. (1973b). Aspartokinase in Lemna minor L. Studies on the in vivo and in vitro regulation of the enzyme. Plant Physiol. 51:327.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Heremans, B., Jacobs, M. A Mutant of Arabidopsis thaliana lpar;L.) Heynh. with Modified Control of Aspartate Kinase by Threonine. Biochem Genet 35, 139–153 (1997). https://doi.org/10.1023/A:1022265825402

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1023/A:1022265825402

Navigation