title: A novel role for protein farnesylation in plant innate immunity.
abstract: Plants utilize tightly regulated mechanisms to defend themselves against pathogens. Initial recognition results in activation of specific Resistance (R) proteins that trigger downstream immune responses, in which the signaling networks remain largely unknown. A point mutation in SUPPRESSOR OF NPR1 CONSTITUTIVE1 (SNC1), a RESISTANCE TO PERONOSPORA PARASITICA4 R gene homolog, renders plants constitutively resistant to virulent pathogens. Genetic suppressors of snc1 may carry mutations in genes encoding novel signaling components downstream of activated R proteins. One such suppressor was identified as a novel loss-of-function allele of ENHANCED RESPONSE TO ABSCISIC ACID1 (ERA1), which encodes the beta-subunit of protein farnesyltransferase. Protein farnesylation involves attachment of C15-prenyl residues to the carboxyl termini of specific target proteins. Mutant era1 plants display enhanced susceptibility to virulent bacterial and oomycete pathogens, implying a role for farnesylation in basal defense. In addition to its role in snc1-mediated resistance, era1 affects several other R-protein-mediated resistance responses against bacteria and oomycetes. ERA1 acts partly independent of abscisic acid and additively with the resistance regulator NON-EXPRESSOR OF PR GENES1 in the signaling network. Defects in geranylgeranyl transferase I, a protein modification similar to farnesylation, do not affect resistance responses, indicating that farnesylation is most likely specifically required in plant defense signaling. Taken together, we present a novel role for farnesyltransferase in plant-pathogen interactions, suggesting the importance of protein farnesylation, which contributes to the specificity and efficacy of signal transduction events.
authors.affiliation: Michael Smith Laboratories , University of British Columbia, Vancouver, British Columbia, Canada V6T 1Z4.
authors.forename: Sandra
authors.initials: S
authors.lastname: Goritschnig
authors.forename: Tabea
authors.initials: T
authors.lastname: Weihmann
authors.forename: Yuelin
authors.initials: Y
authors.lastname: Zhang
authors.forename: Pierre
authors.initials: P
authors.lastname: Fobert
authors.forename: Peter
authors.initials: P
authors.lastname: McCourt
authors.forename: Xin
authors.initials: X
authors.lastname: Li
mesh_terms: D000040:Abscisic Acid / Q000378:metabolism; D019883:Alkyl and Aryl Transferases / Q000378:metabolism; D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000235:genetics / Q000276:immunology* / Q000378:metabolism; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism*; D001483:Base Sequence; D018387:Codon, Initiator; D051231:Farnesyltranstransferase / Q000235:genetics / Q000378:metabolism; D007113:Immunity, Innate; D008969:Molecular Sequence Data; D009154:Mutation; D010935:Plant Diseases / Q000276:immunology*; D017368:Protein Prenylation; D015398:Signal Transduction
chemical_list: D029681:Arabidopsis Proteins; D018387:Codon, Initiator; C411293:ERA1 protein, Arabidopsis; C105496:NPR1 protein, Arabidopsis; C482739:SNC1 protein, Arabidopsis; D000040:Abscisic Acid; D019883:Alkyl and Aryl Transferases; C083291:geranylgeranyltransferase type-I; D051231:Farnesyltranstransferase