NB-LRRs work a "bait and switch" on pathogens.
Plant genomes encode large numbers of highly variable nucleotide binding leucine-rich repeat (NB-LRR) disease resistance proteins. These proteins have been studied extensively to understand their evolution and the molecular basis of their function. Multiple studies indicate that the C-terminal LRR domain plays a pivotal role in defining pathogen recognition specificity. However, a growing body of evidence suggests that the N-termini of NB-LRR proteins also function in pathogen recognition. To formulate a framework that can explain the underlying principles governing NB-LRR function while accommodating findings from different experimental systems, we present a "bait and switch" model. This model proposes a two-step recognition process involving interactions with both cellular cofactors (bait) and the LRR domain, which in turn activates the molecular switch leading to disease resistance.
Collier
Sarah M
SM
Boyce Thompson Institute for Plant Research, Ithaca, NY 14853, USA.
Moffett
Peter
P
D007113:Immunity, Innate / Q000235:genetics / Q000502:physiology; D000090263:Leucine-Rich Repeat Proteins; D008954:Models, Biological; D010940:Plant Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D017434:Protein Structure, Tertiary / Q000235:genetics / Q000502:physiology; D011506:Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism / Q000502:physiology*
D000090263:Leucine-Rich Repeat Proteins; D010940:Plant Proteins; D011506:Proteins