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PLANTS INTERACTING WITH OTHER ORGANISMS

A Novel Role for Protein Farnesylation in Plant Innate Immunity^{1,[C],[W],[OA]}

Michael Smith Laboratories (S.G., T.W., Y.Z., X.L.) and Department of Botany (S.G., T.W., X.L.), University of British Columbia, Vancouver, British Columbia, Canada V6T 1Z4; National Institute of Biological Sciences, Beijing 102206, People's Republic of China (Y.Z.); National Research Council, Plant Biotechnology Institute, Saskatoon, Saskatchewan, Canada S7N 0W9 (P.F.); and Department of Botany, University of Toronto, Toronto, Ontario, Canada M5S 3B2 (P.M.)

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 β-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.

² Present address: Department of Plant and Microbial Biology, 111 Koshland Hall, University of California, Berkeley, CA 94720–3102.

The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantphysiol.org) is: Xin Li (xinli{at}interchange.ubc.ca).

^[C] Some figures in this article are displayed in color online but in black and white in the print edition.

^[W] The online version of this article contains Web-only data.

^[OA] Open Access articles can be viewed online without a subscription.

www.plantphysiol.org/cgi/doi/10.1104/pp.108.117663

^* Corresponding author; e-mail xinli{at}interchange.ubc.ca.

Received February 14, 2008; accepted June 20, 2008; published July 3, 2008.

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On the Inside

Peter V. Minorsky
Plant Physiol. 2008 148: 1-2. [Full Text]