Actinonin-induced inhibition of plant peptide deformylase: A paradigm for the design of novel broad-spectrum herbicides

Cai Xia Hou, Mark Williams

Research output: Chapter in Book/Report/Conference proceedingConference contributionpeer-review

3 Scopus citations


Peptide deformylase, which catalyzes the removal of N-formyl groups from the initiating N-formyl-methionine of nascent polypeptides, has recently been characterized from several plants, including rice, tomato and Arabidopsis thaliana. The two Arabidopsis thaliana DEF genes, AtDEF1 and AtDEF2, encode enzymes which are functionally active both in vitro and in vivo and are catalytically inactivated by the naturally-occurring peptide deformylase inhibitor actinonin, a product of a soil-borne actinomycete. Actinonin has profound herbicidal effects when applied to many plant species both pre- and postemergence. Transgenic tobacco plants were engineered to over-express each of the AtDEF proteins. These plants were completely resistant to the herbicidal effects of actinonin. This data provides the first unequivocal evidence that the lethality of actinonin to plants in vivo is strictly a consequence of the inhibition of peptide deformylase activity. This work also confirms that peptide deformylase is a valid target for both the development of novel broad-spectrum herbicides, and the engineering of herbicide selectivity in plants without the use of foreign genes.

Original languageEnglish
Title of host publicationNatural Products for Pest Management
EditorsAgnes Rimando, Stephen Duke
Number of pages12
StatePublished - 2006

Publication series

NameACS Symposium Series
ISSN (Print)0097-6156

ASJC Scopus subject areas

  • General Chemistry
  • General Chemical Engineering


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