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Published on July 3, 2008; 10.1104/pp.108.117663

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Received February 14, 2008
Accepted June 20, 2008

A novel role for protein farnesylation in plant innate immunity

Sandra Goritschnig , Tabea Weihmann , Yuelin Zhang , Pierre Fobert , Peter McCourt , and Xin Li *

Michael Smith Laboratories, Room 301, 2185 East Mall, University of British Columbia, Vancouver, BC, V6T 1Z4, Canada; Dept. of Botany, Room 3529, 6270 University Blvd., University of British Columbia, Vancouver, BC, V6T 1Z4, Canada; National Institute of Biological Sciences, Zhongguancun Life Science Park, 7 Science Park Road, Beijing 102206, People's Republic of China; National Research Council, Plant Biotechnology Institute, 110 Gymnasium Place, Saskatoon, SK, S7N 0W9, Canada; Dept. of Botany, University of Toronto, 25 Willcocks Street, Toronto, ON, M5S 3B2 Canada

* Corresponding author; email: xinli{at}interchange.ubc.ca.

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 signalling networks remain largely unknown. A point mutation in SNC1, an RPP4 R gene homolog, renders plants constitutively resistant to virulent pathogens. Genetic suppressors of snc1 may carry mutations in genes encoding novel signalling components downstream of activated R proteins. One such suppressor was identified as a novel loss-of-function allele of ENHANCED RESPONSE TO ABSCISIC ACID 1 (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 defence. 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-GENES 1 (NPR1) in the signalling 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 defence signalling. 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.






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