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Published on May 3, 2007; 10.1104/pp.106.094912

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Received December 18, 2006
Accepted April 30, 2007

A Single Binding Site Mediates Resistance- and Disease-Associated Activities of the Effector Protein NIP1 from the Barley Pathogen Rhynchosporium secalis

Klaas A. E. van ‘t Slot , Angela Gierlich , and Wolfgang Knogge *

Department of Stress and Developmental Biology, Leibniz Institute of Plant Biochemistry, D-06210 Halle, Germany

* Corresponding author; email: wknogge{at}ipb-halle.de.

The effector protein NIP1 from the barley pathogen Rhynchosporium secalis specifically induces the synthesis of defense-related proteins in cultivars of barley (Hordeum vulgare L.) expressing the complementary resistance gene, Rrs1. In addition, it stimulates the activity of the barley plasma membrane H+-ATPase in a genotype-unspecific manner and it induces necrotic lesions in leaf tissues of barley and other cereal plant species. The NIP1 variants type I and II, which display quantitative differences in their activities as elicitor and H+-ATPase stimulator, and the inactive mutant variants type III* and type IV* were produced in E. coli. Binding studies using 125I-NIP1 type I revealed a single class of binding sites with identical binding characteristics in microsomes from near-isogenic resistant (Rrs1) and susceptible (rrs1) barley. Binding was specific, reversible and saturable and saturation ligand binding experiments yielded a Kd of 5.6 nM. A binding site was also found in rye and the non-host species wheat, oat and maize, but not in Arabidopsis thaliana. For NIP1 types I and II equilibrium competition binding experiments revealed a correlation between the difference in their affinities to the binding site and the differences in their elicitor activity and H+-ATPase stimulation indicating a single target molecule to mediate both activities. In contrast, the inactive proteins type III* and type IV* are both characterized by high affinities similar to type I suggesting that binding of NIP1 to this target is not sufficient for its activities.






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