title: RAR1 positively controls steady state levels of barley MLA resistance proteins and enables sufficient MLA6 accumulation for effective resistance.
abstract: The polymorphic barley (Hordeum vulgare) Mla locus harbors allelic race-specific resistance (R) genes to the powdery mildew fungus Blumeria graminis f sp hordei. The highly sequence-related MLA proteins contain an N-terminal coiled-coil structure, a central nucleotide binding (NB) site, a Leu-rich repeat (LRR) region, and a C-terminal non-LRR region. Using transgenic barley lines expressing epitope-tagged MLA1 and MLA6 derivatives driven by native regulatory sequences, we show a reversible and salt concentration-dependent distribution of the intracellular MLA proteins in soluble and membrane-associated pools. A posttranscriptional process directs fourfold greater accumulation of MLA1 over MLA6. Unexpectedly, in rar1 mutant plants that are compromised for MLA6 but not MLA1 resistance, the steady state level of both MLA isoforms is reduced. Furthermore, differential steady state levels of MLA1/MLA6 hybrid proteins correlate with their requirement for RAR1; the RAR1-independent hybrid protein accumulates to higher levels and the RAR1-dependent one to lower levels. Interestingly, yeast two-hybrid studies reveal that the LRR domains of RAR1-independent but not RAR1-dependent MLA isoforms interact with SGT1, a RAR1 interacting protein required for the function of many NB-LRR type R proteins. Our findings implicate the existence of a conserved mechanism to reach minimal NB-LRR R protein thresholds that are needed to trigger effective resistance responses.
authors.affiliation: Max-Planck-Institut für Züchtungsforschung, Department of Plant Microbe Interactions, D-50829 Köln, Germany.
authors.forename: Stéphane
authors.initials: S
authors.lastname: Bieri
authors.forename: Stefan
authors.initials: S
authors.lastname: Mauch
authors.forename: Qian-Hua
authors.initials: QH
authors.lastname: Shen
authors.forename: Jack
authors.initials: J
authors.lastname: Peart
authors.forename: Alessandra
authors.initials: A
authors.lastname: Devoto
authors.forename: Catarina
authors.initials: C
authors.lastname: Casais
authors.forename: Francesca
authors.initials: F
authors.lastname: Ceron
authors.forename: Sabine
authors.initials: S
authors.lastname: Schulze
authors.forename: Hans-Henning
authors.initials: HH
authors.lastname: Steinbiss
authors.forename: Ken
authors.initials: K
authors.lastname: Shirasu
authors.forename: Paul
authors.initials: P
authors.lastname: Schulze-Lefert
mesh_terms: D029681:Arabidopsis Proteins / Q000378:metabolism; D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism*; D018797:Cell Cycle Proteins / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism; D015536:Down-Regulation / Q000235:genetics; D005658:Fungi / Q000502:physiology; D006706:Homeostasis / Q000502:physiology; D001467:Hordeum / Q000235:genetics* / Q000378:metabolism* / Q000382:microbiology; D006790:Host-Parasite Interactions / Q000502:physiology; D007113:Immunity, Innate / Q000235:genetics / Q000502:physiology*; D047908:Intracellular Signaling Peptides and Proteins; D010935:Plant Diseases / Q000235:genetics / Q000382:microbiology; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism*; D030821:Plants, Genetically Modified / Q000235:genetics / Q000378:metabolism / Q000382:microbiology; D020033:Protein Isoforms / Q000235:genetics / Q000378:metabolism; D017434:Protein Structure, Tertiary / Q000502:physiology; D012323:RNA Processing, Post-Transcriptional / Q000502:physiology; D015854:Up-Regulation / Q000235:genetics
chemical_list: D029681:Arabidopsis Proteins; D002352:Carrier Proteins; D018797:Cell Cycle Proteins; D047908:Intracellular Signaling Peptides and Proteins; C433105:MLA1 protein, Hordeum vulgare; C430705:MLA6 protein, Hordeum vulgare; D010940:Plant Proteins; D020033:Protein Isoforms; C499582:Rar1 protein, Hordeum vulgare; C452191:SGT1a protein, Arabidopsis