1. Activation of an atypical plant NLR with an N-terminal deletion initiates cell death at the vacuole.
- Author
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Sunil S, Beeh S, Stöbbe E, Fischer K, Wilhelm F, Meral A, Paris C, Teasdale L, Jiang Z, Zhang L, Urban M, Aguilar Parras E, Nürnberger T, Weigel D, Lozano-Duran R, and El Kasmi F
- Subjects
- NLR Proteins genetics, NLR Proteins metabolism, Sequence Deletion, Plant Immunity genetics, Protein Domains, Amino Acid Sequence, Vacuoles metabolism, Arabidopsis genetics, Arabidopsis metabolism, Cell Death genetics, Arabidopsis Proteins genetics, Arabidopsis Proteins metabolism
- Abstract
Plants evolve nucleotide-binding leucine-rich repeat receptors (NLRs) to induce immunity. Activated coiled-coil (CC) domain containing NLRs (CNLs) oligomerize and form apparent cation channels promoting calcium influx and cell death, with the alpha-1 helix of the individual CC domains penetrating the plasma membranes. Some CNLs are characterized by putative N-myristoylation and S-acylation sites in their CC domain, potentially mediating permanent membrane association. Whether activated Potentially Membrane Localized NLRs (PMLs) mediate cell death and calcium influx in a similar way is unknown. We uncovered the cell-death function at the vacuole of an atypical but conserved Arabidopsis PML, PML5, which has a significant deletion in its CC
G10/GA domain. Active PML5 oligomers localize in Golgi membranes and the tonoplast, alter vacuolar morphology, and induce cell death, with the short N-terminus being sufficient. Mutant analysis supports a potential role of PMLs in plant immunity. PML5-like deletions are found in several Brassicales paralogs, pointing to the evolutionary importance of this innovation. PML5, with its minimal CC domain, represents the first identified CNL utilizing vacuolar-stored calcium for cell death induction., (© 2024. The Author(s).)- Published
- 2024
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