A growing body of evidence indicates that elicitation of primary active defense responses results from a recognition event frequently involving protein-protein interactions. Most pathogen avirulence determinants eliciting resistance gene–dependent responses have been shown to be proteins with no apparent enzymic activity. Disruption of the tertiary and quaternary structure of these proteins abolishes their elicitor activity. Critical to their elicitor activity is their display by the pathogen. Resistance genes are proposed to function as receptors for the eliciting proteins. The most consistent feature of resistance gene products is the presence of potential protein binding domains in the form of leucine-rich repeat regions, and there is direct evidence for the physical interaction of elicitor proteins and receptor proteins in several cases. Thus in many but not all cases the primary recognition event eliciting an active defense response during incompatible interactions appears to be a protein-protein interaction occurring between a specific pathogen protein and a strategically placed receptor protein in the host cell. The interaction of elicitor protein with the receptor protein activates a signal transduction pathway leading to programmed cell death and an oxidative burst.


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  • Article Type: Review Article
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