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.
Article PDF
Avoid common mistakes on your manuscript.
References
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).
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).
Egin-Buhler B, Ebel J: Improved purification and further characterization of ACC from culture cells of parsley. Eur J Biochem 133: 335–339 (1983).
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).
Fernandez MD, Lamppa GK: Acyl carrier protein import into chloroplasts. J Biol Chem 266: 7220–7226 (1991).
Harwood JL: Fatty acid metabolism. Annu Rev Plant Physiol Plant Mol Biol 39: 101–138 (1988).
Jahnen-Dechent W, Simpson RJ: A method for preparing proteins and peptides for microsequencing. Plant Mol Biol Rep 8: 92–103 (1990).
Li S, Cronan JE: The gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase. J Biol Chem 267: 855–863 (1992).
Li S, Cronan JE: The genes encoding the two carboxyltransferase subunits of Escherichia coli acetyl-CoA carboxylase. J Biol Chem 267: 16841–16847 (1992).
Lichtenthaler HK: Mode of action of herbicides affecting acetyl-CoA carboxylase and fatty acid biosynthesis. Z Naturforsch 45c: 521–528 (1990).
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).
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).
Maniatis T, Fritsch EF, Sambrook J: Molecular Cloning: A Laboratory Manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY (1982).
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).
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).
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).
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).
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).
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).
Author information
Authors and Affiliations
Rights 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
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00015984