Plant Molecular Biology

, Volume 35, Issue 3, pp 377–381

Expression of chalcone synthase and chalcone isomerase proteins in Arabidopsis seedlings

Authors

  • Cody C. Cain
    • Department of BiologyVirginia Polytechnic Institute and State University
  • David E. Saslowsky
    • Department of BiologyVirginia Polytechnic Institute and State University
  • Richard A. Walker
    • Department of BiologyVirginia Polytechnic Institute and State University
  • Brenda W. Shirley*
    • Department of BiologyVirginia Polytechnic Institute and State University
Article

DOI: 10.1023/A:1005846620791

Cite this article as:
Cain, C.C., Saslowsky, D.E., Walker, R.A. et al. Plant Mol Biol (1997) 35: 377. doi:10.1023/A:1005846620791

Abstract

Antibodies have been developed against the first two enzymes of flavonoid biosynthesis in Arabidopsis thaliana. Chalcone synthase (CHS) and chalcone isomerase (CHI) were overexpressed and purified from Escherichia coli as fusion proteins with glutathione S-transferase from Schistosoma japonicum. The recombinant proteins were then used to immunize chickens and the resulting IgY fraction was purified from egg yolks. Immunoblots of crude protein extracts from Arabidopsis seedlings carrying wild-type and null alleles for CHS and CHI showed that the resulting antibody preparations provide useful tools for characterizing expression of the flavonoid pathway at the protein level. An initial analysis of expression patterns in seedlings shows that CHS and CHI proteins are present at high levels during a brief period of early seedling germination that just precedes the transient accumulation of flavonoid end-products.

Arabidopsischalcone synthasechalcone isomeraseflavonoidsfusion proteinspolyclonal antibodies

Copyright information

© Kluwer Academic Publishers 1997