How plant lysin motif receptors get activated: lessons learned from structural biology.

Lysin motif (LysM) receptor kinases are unique to plants and serve important functions in plant-microbe interactions. These proteins recognize microbe-derived N-acetylglucosamine (NAG)-containing ligands, but the molecular mode of ligand perception and of receptor activation has remained unknown. The three-dimensional structure of the LysM receptor kinase CERK1 (chitin elicitor receptor kinase 1) from Arabidopsis thaliana has been reported.

Separable roles of the Pseudomonas syringae pv. phaseolicola accessory protein HrpZ1 in ion-conducting pore formation and activation of plant immunity.

The HrpZ1 gene product from phytopathogenic Pseudomonas syringae is secreted in a type-III secretion system-dependent manner during plant infection. The ability of HrpZ1 to form ion-conducting pores is proposed to contribute to bacterial effector delivery into host cells, or may facilitate the nutrition of bacteria in the apoplast. Furthermore, HrpZ1 is reminiscent of a pathogen-associated molecular pattern (PAMP) that triggers immunity-associated responses in a variety of plants.

The Arabidopsis AtPNG1 gene encodes a peptide: N-glycanase.

Deglycosylation of misfolded proteins by the endoplasmic reticulum-associated degradation (ERAD) pathway is catalyzed by peptide:N-glycanases (PNGases) that are highly conserved among mammals and yeast. The catalytic mechanism of PNGases employs a catalytic triad consisting of Cys, His and Asp residues, which is shared by other enzyme families such as cysteine proteases and protein cross-linking transglutaminases (TGases). In contrast to the yeast and mammalian systems, very little is known about ERAD in plants and the enzymes responsible for proper clearance of misfolded plant proteins.