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Published on November 5, 2008; 10.1104/pp.108.130732

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Received October 2, 2008
Accepted October 31, 2008

The genetic basis of constitutive and herbivore-induced ESP-independent nitrile formation in Arabidopsis thaliana

Meike Burow , Anja Losansky , Rene Muller , Antje Plock , Daniel J. Kliebenstein , and Ute Wittstock *

Institut fur Pharmazeutische Biologie, Technische Universitat Braunschweig, Mendelssohnstrasse 1, 38106 Braunschweig, Germany; Department of Plant Sciences, University of California, Davis, One Shields Avenue, Davis, CA 95616

* Corresponding author; email: u.wittstock{at}tu-bs.de.

Glucosinolates are a group of thioglucosides that are components of an activated chemical defense found in the Brassicales. Plant tissue damage results in hydrolysis of glucosinolates by endogenous thioglucosidases known as myrosinases. Spontaneous rearrangement of the aglucone yields reactive isothiocyanates that are toxic to many organisms. In the presence of specifier proteins, alternative products, namely epithionitriles, simple nitriles and thiocyanates with different biological activities are formed at the expense of isothiocyanates. Recently, simple nitriles have been recognized to serve distinct functions in plant-insect interactions. Here, we show that simple nitrile formation in Arabidopsis thaliana Col-0 rosette leaves increases in response to herbivory, and that this increase is independent of the known epithiospecifier protein (ESP). We combined phylogenetic analysis, a screen of A. thaliana mutants, recombinant protein characterization, and expression QTL-mapping to identify a gene encoding a nitrile-specifier protein (NSP) responsible for constitutive and herbivore-induced simple nitrile formation in Col-0 rosette leaves. AtNSP1 is one out of five A. thaliana ESP homologues that promote simple nitrile, but not epithionitrile or thiocyanate formation. Four of these homologues possess one or two lectin-like jacalin domains which share a common ancestry with the jacalin domains of the putative A. thaliana myrosinase-binding proteins MBP1 and MBP2. A sixth ESP homologue lacked specifier activity and likely represents the ancestor of the gene family with a different biochemical function. By illuminating the genetic and biochemical bases of simple nitrile formation, our study allows new insights into the evolution of metabolic diversity in a complex plant defense system.




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[Abstract] [Full Text] [PDF]


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