Skip to main content
SpringerLink
Log in

A single amino acid change in acetolactate synthase confers resistance to valine in tobacco

  • Original Paper
  • Published:
Molecular and General Genetics MGG Aims and scope Submit manuscript

Abstract

The metabolic control of branched chain amino acid (BCAA) biosynthesis involves allosteric regulation of acetolactate synthase (ALS) by the end-products of the pathway, valine, leucine and isoleucine. We describe here the molecular basis of valine resistance. We cloned and sequenced an ALS gene from the tobacco mutant Valr-1 and found a single basepair substitution relative to the wild-type allele. This mutation causes a serine to leucine change in the amino acid sequence of ALS at position 214. We then mutagenized the wild-type allele of the ALS gene ofArabidopsis and found that it confers valine resistance when introduced into tobacco plants. Taken together, these results suggest that the serine to leucine change at position 214 of ALS is responsible for valine resistance in tobacco.

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

Access this article

Log in via an institution

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

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  • Bourgin JP (1978) Valine-resistant plants from in vitro selected tobacco cells. Mol Gen Genet 161:225–230

    Google Scholar 

  • Bourgin JP, Chupeau Y, Missonier C (1979) Plant regeneration from mesophyll protoplasts of severalNicotiana species. Physiol Plant 45:288–292

    Google Scholar 

  • Bourgin JP, Goujaud J, Missonier C, Pethe C (1985) Valine resistance, a potential marker in plant cell genetics. I. Distinction between two types of valine-resistant tobacco mutants isolated from protoplast-derived cells. Genetics 109:393–407

    Google Scholar 

  • Boutry M, Chua NH (1985) A nuclear gene encoding the beta subunit of the mitochondrial ATP synthase inNicotiana plumbaginifolia. EMBO J 4:2159–2165

    PubMed  Google Scholar 

  • Chaleff RS, Ray TB (1984) Herbicide-resistant mutants from tobacco cell cultures. Science 223:1148–1151

    Google Scholar 

  • Hattori J, Rutledge R, Labbé H, Brown D, Sunohara G, Miki B (1992) Multiple resistance to sulfonylureas and imidazolinones conferred by an acetohydroxyacid synthase gene with separate mutations for selective resistance. Mol Gen Genet 232:167–173

    PubMed  Google Scholar 

  • Haughn GW, Somerville C (1986) Sulfonylurea-resistant mutants ofArabidopsis thaliana. Mol Gen Genet 204:430–434

    Google Scholar 

  • Haughn GW, Somerville C (1990) A mutation causing imidazolinone resistance maps to theCSR1 locus ofArabidopsis thaliana. Plant Physiol 92:1081–1085

    Google Scholar 

  • Haughn GW, Smith J, Mazur B, Somerville C (1988) Transformation with a mutantArabidopsis acetolactate synthase gene renders tobacco resistant to sulfonylurea herbicides. Mol Gen Genet 211:266–271

    Google Scholar 

  • Hawkes TJ, Howard JL, Pontin SE (1989) Herbicides that inhibit the biosynthesis of branched chain amino acids. In: Dodge A (ed) Herbicides and plant metabolism. Cambridge Academic, Cambridge, pp 112–126

    Google Scholar 

  • Kunkel TA (1985) Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc Natl Acad Sci USA 82:488–492

    PubMed  Google Scholar 

  • Lee KY, Townsend J, Tepperman J, Black M, Chui CF, Mazur B, Dunsmuir P, Bedbrook J (1988) The molecular basis of sulfonylurea herbicide resistance in tobacco. EMBO J 7:1241–1248

    Google Scholar 

  • Mazur BJ, Chui C-F, Smith JK (1987) Isolation and characterization of plant gene coding for acetolactate synthase, the target enzyme for two classes of herbicides. Plant Physiol 85:1110–1117

    Google Scholar 

  • Mazur B, Falco SC (1989) The development of herbicide-resistant crops. Annu Rev Plant Physiol Plant Mol Biol 40:441–470

    Google Scholar 

  • Miflin BJ (1969) Acetolactate synthase from barley seedlings. Phytochem 8:2271–2276

    Google Scholar 

  • Miflin BJ (1971) Cooperative feedback control of barley acetohydroxy acid synthase by leucine, isoleucine and valine. Arch Biochem Biophys 146:542–550

    PubMed  Google Scholar 

  • Mourad G, Pandey B, King J (1993) Isolation and genetic analysis of a triazolopyrimidine-resistant mutant ofArabidopsis. J Heredity 84:91–96

    Google Scholar 

  • Rathinasabapathi B, King J (1992) Physiological response of herbicide-resistant variants ofDatura innoxia to branched chain amino acids. Plant Sci 81:191–198

    Google Scholar 

  • Rathinasabapathi B, Williams D, King J (1990) Altered feedback sensitivity to valine, leucine and isoleucine of acetolactate synthase from herbicide-resistant variants ofDatura innoxia. Plant Sci 67:1–6

    Google Scholar 

  • Ray T (1984) Site of action of chlosulfuron: inhibition of valine and isoleucine biosynthesis in plants. Plant Physiol 75:827–831

    Google Scholar 

  • Relton JM, Wallsgrove RM, Bourgin JP, Bright SWJ (1986) Altered feedback sensitivity of acetohydroxyacid synthase from valine-resistant mutants of tobacco (Nicotiana tabacum L.). Planta 169:46–50

    Google Scholar 

  • Rogers SG, Horsch RB, Fraley RT (1986) Gene transfer in plants: production of transformed plants using Ti plasmid vectors. Methods Enzymol 118:627–640

    Google Scholar 

  • Schulze-Siebert D, Heineke D, Scharf H, Schultz G (1984) Pyruvatederived amino acids in spinach chloroplasts: synthesis and regulation during photosynthetic carbon metabolism. Plant Physiol 76:465–471

    Google Scholar 

  • Shaner DL, Anderson PC, Stidham MA (1984) Imidazolinones: potent inhibitors of acetohydroxyacid synthase. Plant Physiol 76:545–546

    Google Scholar 

  • Subramanian MV, Loney-Gallant V, Dias JM, Mireles LC (1991) Acetolactate synthase inhibiting herbicides bind to the regulatory site. Plant Physiol 96:310–313

    Google Scholar 

  • Tourneur C, Jouanin L, Vaucheret H (1993) Over-expression of acetolactate synthase confers resistance to valine in transgenic tobacco plants. Plant Sci 88:159–168

    Google Scholar 

  • Vieira J, Messing J (1987) Production of single-stranded plasmid DNA. Methods Enzymol 153:3–11

    PubMed  Google Scholar 

  • Yadav N, McDevitt RE, Benard S, Falco SC (1986) Single amino acid substitutions in the enzyme acetolactate synthase confer resistant to the herbicide sulfometuron methyl. Proc Natl Acad Sci USA 83:4418–4422

    Google Scholar 

  • Wu K, Mourad G, King J (1994) A valine-resistant mutant ofArabidopsis thaliana displays an acetolactate synthase with altered feedback control. Planta 192:249–255

    Google Scholar 

  • Zhou C, Abaigar L, Jong AY (1990) A protocol for using T7 DNA polymerase in oligonucleotide site-directed mutagenesis. Bio-Techniques 8:503

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Laboratoire de Biologie Cellulaire, INRA, F-78026, Versailles Cedex, France

    F. Hervieu & H. Vaucheret

Authors
  1. F. Hervieu
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. H. Vaucheret
    View author publications

    You can also search for this author in PubMed Google Scholar

Additional information

Communicated by A. Kondorosi

This paper is dedicated to the memory of Jean-Pierre Bourgin, who died on October 29, 1994, at the age of 50

Rights and permissions

Reprints and permissions

About this article

Cite this article

Hervieu, F., Vaucheret, H. A single amino acid change in acetolactate synthase confers resistance to valine in tobacco. Molec. Gen. Genet. 251, 220–224 (1996). https://doi.org/10.1007/BF02172921

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF02172921

Keywords

Search

Navigation