title: The TIR domain of TIR-NB-LRR resistance proteins is a signaling domain involved in cell death induction.
abstract: In plants, the TIR (toll interleukin 1 receptor) domain is found almost exclusively in nucleotide-binding (NB) leucine-rich repeat resistance proteins and their truncated homologs, and has been proposed to play a signaling role during resistance responses mediated by TIR containing R proteins. Transient expression in Nicotiana benthamiana leaves of "TIR + 80", the RPS4 truncation without the NB-ARC domain, leads to EDS1-, SGT1-, and HSP90-dependent cell death. Transgenic Arabidopsis plants expressing the RPS4 TIR+80 from either dexamethasone or estradiol-inducible promoters display inducer-dependent cell death. Cell death is also elicited by transient expression of similarly truncated constructs from two other R proteins, RPP1A and At4g19530, but is not elicited by similar constructs representing RPP2A and RPP2B proteins. Site-directed mutagenesis of the RPS4 TIR domain identified many loss-of-function mutations but also revealed several gain-of function substitutions. Lack of cell death induction by the E160A substitution suggests that amino acids outside of the TIR domain contribute to cell death signaling in addition to the TIR domain itself. This is consistent with previous observations that the TIR domain itself is insufficient to induce cell death upon transient expression.
authors.affiliation: Sainsbury Laboratory, John Innes Centre, Norwich Research Park, Norwich, UK.
authors.forename: Michal R
authors.initials: MR
authors.lastname: Swiderski
authors.forename: Doris
authors.initials: D
authors.lastname: Birker
authors.forename: Jonathan D G
authors.initials: JD
authors.lastname: Jones
mesh_terms: D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D017360:Arabidopsis / Q000166:cytology* / Q000235:genetics / Q000378:metabolism; D016923:Cell Death; D018506:Gene Expression Regulation, Plant; D000090263:Leucine-Rich Repeat Proteins; D008969:Molecular Sequence Data; D016296:Mutagenesis; D050505:Mutant Proteins / Q000378:metabolism; D009154:Mutation / Q000235:genetics; D018515:Plant Leaves / Q000166:cytology / Q000382:microbiology; D010940:Plant Proteins / Q000737:chemistry* / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D036226:Seedlings / Q000166:cytology; D016415:Sequence Alignment; D015398:Signal Transduction; D014026:Nicotiana / Q000166:cytology* / Q000235:genetics / Q000378:metabolism / Q000382:microbiology
chemical_list: D000090263:Leucine-Rich Repeat Proteins; D050505:Mutant Proteins; D010940:Plant Proteins; D011506:Proteins; C097421:rps4 protein, plant