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Identification of Post-translational Modifications of Plant Protein Complexes
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How to build a pathogen detector: structural basis of NB-LRR function.

Frank L W Takken1, Aska Goverse

  • 1University of Amsterdam, SILS, Molecular Plant Pathology, Science Park 904, 1098 XH Amsterdam, The Netherlands. f.l.w.takken@uva.nl

Current Opinion in Plant Biology
|June 5, 2012
PubMed
Summary

Plant disease resistance proteins, nucleotide-binding leucine-rich repeats (NB-LRRs), act as pathogen detectors. Recent structural insights reveal how their multi-domain architecture enables defense signaling while maintaining auto-inhibition.

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Area of Science:

  • Plant pathology
  • Molecular biology
  • Structural biology

Background:

  • Plant disease resistance (R) proteins, particularly nucleotide-binding leucine-rich repeat (NB-LRR) proteins, are crucial for recognizing pathogen effectors and initiating host defense.
  • The multi-domain structure of NB-LRRs integrates sensing, switching, and response functions for pathogen detection.

Purpose of the Study:

  • To review operational models of NB-LRR functioning.
  • To integrate recent structural insights into the understanding of NB-LRR mechanisms.

Main Methods:

  • Review of structure-function analyses of NB-LRR proteins.
  • Elucidation of 3D structures of NB-LRR subdomains.
  • Analysis of interactions with chaperones, proteasomes, and effector targets.

Main Results:

  • NB-LRR multi-domain structure facilitates pathogen recognition and defense activation.
  • Individual subdomains contribute distinct functions within the NB-LRR protein.
  • Interactions with accessory factors maintain NB-LRRs in a poised, auto-inhibited state.

Conclusions:

  • Recent structural advances provide new insights into NB-LRR operational models.
  • Understanding NB-LRR structure is key to deciphering plant immune signaling pathways.