Skip to main content
SpringerLink
Log in

Wheat acetyl-CoA carboxylase

  • Update Section
  • Short Communication
  • Published:
Plant Molecular Biology Aims and scope Submit manuscript

Abstract

The acetyl-CoA carboxylase present in both wheat germ and total wheat leaf protein contains ca. 220 kDa subunits. It is the major biotin-dependent carboxylase present in wheat chloroplasts. Active acetyl-CoA carboxylase purified from wheat germ is a homodimer with an apparent molecular mass of ca. 500 kDa. The enzyme from wheat germ or from wheat chloroplasts is sensitive to the herbicide haloxyfop at micromolar levels. The incorporation of 14C-acetate into fatty acids in freshly cut wheat seedling leaves provides a convenient in vivo assay for both acetyl-CoA carboxylase and haloxyfop.

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

References

  1. Al-feel W, Chirala SS, Wakil SJ: Cloning of the yeast FAS3 gene and primary structure of yeast acetyl-CoA carboxylase. Proc Natl Acad Sci USA 89: 4534–4538 (1992).

    PubMed  Google Scholar 

  2. Alix J-H: A rapid procedure for cloning genes from λ libraries by complementation of E. coli defective mutants: application to the fabE region of the E. coli chromosome. DNA 8: 779–789 (1989).

    PubMed  Google Scholar 

  3. Egin-Buhler B, Ebel J: Improved purification and further characterization of ACC from culture cells of parsley. Eur J Biochem 133: 335–339 (1983).

    PubMed  Google Scholar 

  4. Egin-Buhler B, Loyal R, Ebel J: Comparison of acetyl-CoA carboxylase from parsley cell culture and from wheat germ. Arch Biochem Biophys 203: 90–100 (1980).

    PubMed  Google Scholar 

  5. Fernandez MD, Lamppa GK: Acyl carrier protein import into chloroplasts. J Biol Chem 266: 7220–7226 (1991).

    PubMed  Google Scholar 

  6. Harwood JL: Fatty acid metabolism. Annu Rev Plant Physiol Plant Mol Biol 39: 101–138 (1988).

    Article  Google Scholar 

  7. Jahnen-Dechent W, Simpson RJ: A method for preparing proteins and peptides for microsequencing. Plant Mol Biol Rep 8: 92–103 (1990).

    Google Scholar 

  8. Li S, Cronan JE: The gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase. J Biol Chem 267: 855–863 (1992).

    PubMed  Google Scholar 

  9. Li S, Cronan JE: The genes encoding the two carboxyltransferase subunits of Escherichia coli acetyl-CoA carboxylase. J Biol Chem 267: 16841–16847 (1992).

    PubMed  Google Scholar 

  10. Lichtenthaler HK: Mode of action of herbicides affecting acetyl-CoA carboxylase and fatty acid biosynthesis. Z Naturforsch 45c: 521–528 (1990).

    Google Scholar 

  11. Lopez-Casillas F, Bai DH, Luo X, Kong IS, Hermodson MA, Kim KH: Structure of the coding sequence and primary amino acid sequence of rat Acetyl-coenzyme A carboxylase. Proc Natl Acad Sci USA 85: 5784–5788 (1988).

    PubMed  Google Scholar 

  12. Luo X, Park K, Lopez-Casillas F, Kim K: Structural features of acetyl-CoA carboxylase gene: mechanism for the generation of mRNAs with 5′-end heterogeneity. Proc Natl Acad Sci USA 86: 4042–4046 (1989).

    PubMed  Google Scholar 

  13. Maniatis T, Fritsch EF, Sambrook J: Molecular Cloning: A Laboratory Manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY (1982).

    Google Scholar 

  14. Muramatsu S, Mizuno T: Nucleotide sequence of the fabE gene and flanking regions containing a bent DNA sequence of Escherichia coli. Nucl Acids Res 17: 3982 (1989).

    PubMed  Google Scholar 

  15. Rendina AR, Felts JM, Beaudoin JD, Craig-Kennard AC, Look LL, Paraskos SL, Hagenah JA: Kinetic characterization, stereoselectivity and species selectivity of the inhibition of plant acetyl-CoA carboxylase by the aryloxyphenoxypropionic acid grass herbicides. Arch Biochem Biophys 265: 219–225 (1988).

    PubMed  Google Scholar 

  16. Slabas AR, Hellyer A: Rapid purification of a high molecular weight subunit polypeptide form of rape seed acetyl-CoA carboxylase. Plant Sci 39: 177–182 (1985).

    Article  Google Scholar 

  17. Takai T, Yokoyama C, Wada K, Tanabe T: Primary structure of chicken liver acetyl-coenzyme A carboxylase deduced from cDNA sequence. J Biol Chem 263: 2651–2657 (1988).

    PubMed  Google Scholar 

  18. Witters LA, Kemp BE: Insulin activation of acetyl-CoA carboxylase by inhibition of the 5′-AMP-activated protein kinase. J Biol Chem 267: 2864–2867 (1992).

    PubMed  Google Scholar 

  19. Wurtele ES, Nikolau BJ: Plants contain multiple biotin enzymes: discovery of 3-methylcrotonyl-CoA carboxylase, propionyl-CoA carboxylase and pyruvate carboxylase in the plant kingdom. Arch Biochem Biophys 278: 179–186 (1990).

    PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Melecular Genetics and Cell Biology, University of Chicago, 60637, Chicago, IL, USA

    Piotr Gornicki & Robert Haselkorn

Authors
  1. Piotr Gornicki
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Robert Haselkorn
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Gornicki, P., Haselkorn, R. Wheat acetyl-CoA carboxylase. Plant Mol Biol 22, 547–552 (1993). https://doi.org/10.1007/BF00015984

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00015984

Key words

Search

Navigation