Hostname: page-component-78c5997874-4rdpn Total loading time: 0 Render date: 2024-11-14T15:15:51.978Z Has data issue: false hasContentIssue false
  • English
  • Français

Suppression of CtpA in Mouseearcress Produces a Phytotoxic Effect: Validation of CtpA as a Target for Herbicide Development

Published online by Cambridge University Press:  20 January 2017

Yun-Chia Sophia Chen ,
Brad J. Fabbri ,
Claire A. CaJacob ,
John C. Anderson  and
Stephen M. G. Duff
Yun-Chia Sophia Chen
Affiliation:
Monsanto Company, 700 Chesterfield Pkwy North, St. Louis, MO, 63198
Brad J. Fabbri
Affiliation:
Monsanto Company, 700 Chesterfield Pkwy North, St. Louis, MO, 63198
Claire A. CaJacob
Affiliation:
Monsanto Company, 700 Chesterfield Pkwy North, St. Louis, MO, 63198
John C. Anderson
Affiliation:
Monsanto Co, 2111 Piilani Hwy, P.O. Box 629, Kihei, HI 96753
Stephen M. G. Duff*
Affiliation:
Monsanto Company, 700 Chesterfield Pkwy North, St. Louis, MO, 63198
*
Corresponding author's E-mail: [email protected]
Get access Rights & Permissions [Opens in a new window]

Abstract

To validate carboxyterminal processing protease of D1 protein (CtpA) as a target for herbicide discovery, CtpA sense mRNAs were overexpressed to suppress the internal level of CtpA protein in mouseearcress plants. Using antibodies raised against recombinant CtpA protein, we demonstrated that we have generated transgenic mouseearcress plants with reduced levels of CtpA protein and plants with elevated levels of CtpA protein. Transgenic plants with severely reduced levels of CtpA protein exhibited a bleached and chlorotic phenotype and stunted growth. The mutant phenotypes were enhanced by bright illumination. However, plants with a slight reduction of CtpA protein did not exhibit the mutant phenotype and could not be distinguished from wild-type plants under normal growth conditions. Several CtpA enzyme inhibitors were shown to have herbicidal activity in planta. Interestingly, plants producing excessive amount of CtpA protein were shown to be resistant to these inhibitors. Our results suggest that CtpA is essential for plant growth and development, but a reduced amount of CtpA is sufficient to carry out its essential function. CtpA may be a good target for herbicide development, but very high levels of inhibition may be required to produce a herbicidal effect. In addition, overexpressing CtpA in target plants might provide a mechanism for producing plants resistant to the herbicide.

Keywords

CtpA, Carboxyterminal processing protease of D1 protein (also referred to as D1 protease)mouseearcress, Arabidopsis thaliana (L.) HeynhD1 proteasecosuppressionphytotoxicityherbicide targetmode of action
Type
Physiology, Chemistry, and Biochemistry
Information
Weed Science , Volume 55 , Issue 4 , August 2007 , pp. 283 - 287
Copyright
Copyright © Weed Science Society of America 

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Literature Cited

Ahrens, W. H. 1994. Atrazine. in Ahrens, W.H., ed. Herbicide Handbook of the Weed Science Society of America. 7th ed. Champaign, IL Weed Science Society of America.Google Scholar
Anbudurai, P. R., Mor, T. S., Shestakov, S. V., Ohad, I., and Pakrasi, H. B. 1994. The CtpA gene encodes the C-terminal processing protease for the D1 protein of the photosystem II reaction center complex. Proc. Natl. Acad. Sci. USA. 91:8082–8086.Google Scholar
Ausubel, F. M. and Brent, R. 1997. Current Protocols in Molecular Biology. New York J. Wiley.Google Scholar
Depicker, A. and Van Montagu, M. 1997. Post-transcriptional gene silencing in plants. Curr. Opin. Cell Biol. 9:373–382.Google Scholar
Duff, S. M. G., Chen, Y-C. S., and Fabbri, B. et al. 2007. The carboxyterminal processing protease of D1 protein: herbicidal activity of novel inhibitors of the recombinant and native spinach enzymes. Pestic. Biochem. Physiol. 88:1–13.Google Scholar
Fabbri, B. J., Chen, Y-C. S., and Duff, S. M. G. 2002. D1 protease: a model target for herbicide development. Pages 79–99. in Pandalai, S.G. ed. Recent Research Developments in Plant Physiology. Trivandrum, India Research Signpost.Google Scholar
Fabbri, B., Duff, S. M. D., Remsen, E. E., Chen, Y-C. S., Andersen, J. C., and CaJacob, C. A. 2005. The carboxyterminal processing protease of D1 protein: expression, purification and enzymology of the recombinant and native spinach enzymes. Pest. Manag. Sci. 61:682–690.CrossRefGoogle Scholar
Feldmann, K. 1991. T-DNA insertion mutagenesis in Arabidopsis: mutational spectrum. Plant J. 1:71–82.Google Scholar
Fujita, S., Inagaki, N., Yamamoto, Y., Taguchi, F., Matsumoto, A., and Satoh, K. 1995. Identification of the carboxyl-terminal processing protease for the D1 precursor protein of the photosystem II reaction center of spinach. Plant Cell Physiol. 36:1169–1177.Google Scholar
Mattoo, A. K., Pick, U., Hoffman-Falk, H., and Edelman, M. 1981. The rapidly metabolized 32,000-dalton polypeptide of the chloroplast is the “proteinaceous shield” regulating photosystem II electron transport and mediating diuron herbicide sensitivity. Proc. Natl. Acad. Sci. U. S. A. 78:1572–1576.CrossRefGoogle ScholarPubMed
Nixon, P. J., Rogner, M., and Diner, B. A. 1991. Expression of a higher plant psbA gene in Synechocystis 6803 yields a functional hybrid photosystem II reaction center complex. Plant Cell. 3:383–395.Google Scholar
Pfister, K., Steinback, K. E., Gardner, G., and Arntzen, C. J. 1981. Photoaffinity labeling of an herbicide receptor protein in chloroplast membranes. Proc. Natl. Acad. Sci. U. S. A. 78:981–985.CrossRefGoogle ScholarPubMed
Reisfeld, A., Mattoo, A. K., and Edelman, M. 1982. Processing of a chloroplast-translated membrane protein in vivo: analysis of the rapidly synthesized 32 000-dalton shield protein and its precursor in Spirodela oligorrhiza . Eur. J. Biochem. 124:125–129.Google Scholar
Rögner, M., Boekema, E. J., and Barber, J. 1996. How does photosystem II split water? the structural basis of efficient energy conversion. Trends Biochem. Sci. 21:44–49.Google Scholar
Sambrook, J., Fritsch, E. F., and Maniatis, T. 1988. Molecular Cloning: A Laboratory Manual. Cold Spring Harbor, NY Cold Spring Harbor Laboratory.Google Scholar
Taguchi, F., Yamamoto, Y., and Satoh, K. 1995. Recognition of the structure around the site of cleavage by the carboxyl-terminal processing protease for D1 precursor protein of the photosystem II reaction center. J. Biol. Chem. 270:10711–10716.Google Scholar
Taylor, M. A., Packer, J. C. L., and Bowyer, J. R. 1988. Processing of the D1 polypeptide of the photosystem II reaction center and photoactivation of a low fluorescence mutant (LF-1) of Scenedesmus obliquus . FEBS Lett. 237:229–233.CrossRefGoogle Scholar
Trost, J. T., Chisholm, D. A., Jordan, D. B., and Diner, B. A. 1997. The D1 C-terminal processing protease of photosystem II from Scenedesmus obliquus: protein purification and gene characterization in wild type and processing mutants. J. Biol. Chem. 272:20348–20356.CrossRefGoogle ScholarPubMed