Unbound MEDLINE

The phytohormone precursor OPDA is isomerized in the insect gut by a single, specific glutathione transferase. Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] Journal article

 
TitleThe phytohormone precursor OPDA is isomerized in the insect gut by a single, specific glutathione transferase.
Author(s)Dabrowska P, Freitak D, Vogel H, Heckel DG, Boland W 
InstitutionDepartments of Bioorganic Chemistry, and Entomology, Max Planck Institute for Chemical Ecology, D-07745 Jena, Germany.
SourceProc Natl Acad Sci U S A 2009 Sep 22; 106(38):16304-9.
AbstractOxylipins play important roles in stress signaling in plants. The compound 12-oxophytodienoic acid (cis-OPDA) is an early biosynthetic precursor of jasmonic acid (JA), the key phytohormone orchestrating the plant anti-herbivore defense. When consumed by feeding Lepidopteran larvae, plant-derived cis-OPDA suffers rapid isomerization to iso-OPDA in the midgut and is excreted in the frass. Unlike OPDA epimerization (yielding trans-OPDA), the formation of iso-OPDA is enzyme-dependent, and is catalyzed by an inducible glutathione transferase (GSTs) from the larval gut. Purified GST fractions from the gut of Egyptian cotton leafworm (Spodoptera littoralis) and cotton bollworm (Helicoverpa armigera) both exhibited strong OPDA isomerization activity, most likely via transient formation of a glutathione-OPDA conjugate. Out of 16 cytosolic GST proteins cloned from the gut of cotton bollworm larvae and expressed in E. coli, only one catalyzed the OPDA isomerization. The biological function of the double bond shift might be seen in an inactivation of cis-OPDA, similar to the inactivation of prostaglandin A1 to prostaglandin B1 in mammalian tissue. The enzymatic isomerization is particularly widespread among generalist herbivores that have to cope with various amounts of cis-OPDA in their spectrum of host plants.
Languageeng
Pub Type(s)Journal Article
Research Support, Non-U.S. Gov't
PubMed ID19805297
  
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