How to build a pathogen detector: structural basis of NB-LRR function.
Many plant disease resistance (R) proteins belong to the family of nucleotide-binding-leucine rich repeat (NB-LRR) proteins. NB-LRRs mediate recognition of pathogen-derived effector molecules and subsequently activate host defence. Their multi-domain structure allows these pathogen detectors to simultaneously act as sensor, switch and response factor. Structure-function analyses and the recent elucidation of the 3D structures of subdomains have provided new insight in how these different functions are combined and what the contribution is of the individual subdomains. Besides interdomain contacts, interactions with chaperones, the proteasome and effector baits are required to keep NB-LRRs in a signalling-competent, yet auto-inhibited state. In this review we explore operational models of NB-LRR functioning based on recent advances in understanding their structure.
University of Amsterdam, SILS, Molecular Plant Pathology, Science Park 904, 1098 XH Amsterdam, The Netherlands. f.l.w.takken@uva.nl
Frank L W
FL
Takken
Aska
A
Goverse
D001419:Bacteria / Q000378:metabolism; D060467:Disease Resistance / Q000276:immunology*; D054884:Host-Pathogen Interactions / Q000276:immunology*; D051756:Leucine-Responsive Regulatory Protein / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000378:metabolism; D057865:Plant Immunity / Q000502:physiology; D010944:Plants / Q000276:immunology* / Q000382:microbiology*; D011487:Protein Conformation; D015398:Signal Transduction / Q000502:physiology
D018832:Molecular Chaperones; D051756:Leucine-Responsive Regulatory Protein