Plant Physiology Preview
Published on February 17, 2006; 10.1104/pp.105.073510
OPEN ACCESS ARTICLE
Received October 28, 2005
Returned for revision November 10, 2005
Accepted January 26, 2006
Mutations in the NB-ARC domain of I-2 that impair ATP hydrolysis cause autoactivation
Wladimir I.L. Tameling , Jack H. Vossen , Mario Albrecht , Thomas Lengauer , Jan A. Berden , Michel A. Haring , Ben J.C. Cornelissen , and Frank L.W. Takken *
Plant Physiology, Swammerdam Institute for Life Sciences, University of Amsterdam, PO Box 94062, 1090 GB Amsterdam, the Netherlands
Max Planck Institute for Informatics, Stuhlsatzenhausweg 85, 66123 Saarbrücken, Germany
Biomolecular Mass Spectrometry, Swammerdam Institute for Life Sciences, University of Amsterdam, Nieuwe Achtergracht 116, 1018 WV, Amsterdam, the Netherlands
Plant Pathology, Swammerdam Institute for Life Sciences, University of Amsterdam, PO Box 94062, 1090 GB Amsterdam, the Netherlands
* Corresponding author; email: takken{at}science.uva.nl.
Resistance (R) proteins in plants confer specificity to the innate immune system. Most R proteins have a centrally located nucleotide-binding (NB-ARC) domain. For two tomato (Lycopersicon esculentum) R proteins, I-2 and Mi-1, we have previously shown that this domain acts as an ATPase module that can hydrolyze ATP in vitro. To investigate the role of nucleotide- binding and -hydrolysis for the function of I-2 in planta, specific mutations were introduced in conserved motifs of the NB-ARC domain. Two mutations resulted in autoactivating proteins that induce a pathogen-independent hypersensitive response upon expression in planta. These mutant forms of I-2 were found to be impaired in ATP hydrolysis but not in ATP binding, suggesting that the ATP-, rather than the ADP-bound state of I-2 is the active form that triggers defence signalling. In addition, upon ADP binding the protein displayed an increased affinity for ADP suggestive for a change of conformation. Based on these data, we propose that the NB-ARC domain of I-2, and likely of related R proteins, functions as a molecular switch whose state (On/Off) depends on the nucleotide bound (ATP/ADP).
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