Mutations in the NB-ARC domain of I-2 that impair ATP hydrolysis cause 
autoactivation

Tameling, Wladimir I.; Vossen, Jack H.; Albrecht, Mario; Lengauer, Thomas; Berden, Jan A.; Haring, Michel A.; Cornelissen, Ben J.C.; Takken, Frank L. W.

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Mutations in the NB-ARC domain of I-2 that impair ATP hydrolysis cause autoactivation

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Albrecht, Mario
Computational Biology and Applied Algorithmics, MPI for Informatics, Max Planck Society;

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Lengauer, Thomas
Computational Biology and Applied Algorithmics, MPI for Informatics, Max Planck Society;

Takken, Frank L. W.
Max Planck Society;

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引用

Tameling, W. I., Vossen, J. H., Albrecht, M., Lengauer, T., Berden, J. A., Haring, M. A., Cornelissen, B. J., & Takken, F. L. W. (2006). Mutations in the NB-ARC domain of I-2 that impair ATP hydrolysis cause autoactivation. Plant Physiology, 140, 1233-1245.

引用: https://hdl.handle.net/11858/00-001M-0000-000F-2381-1

要旨

Resistance (R) proteins in plants confer specificity to the innate immune system. Most R proteins have a centrally located NB-ARC (nucleotide-binding adaptor shared by APAF-1, R proteins, and CED-4) 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 defense signaling. In addition, upon ADP binding, the protein displayed an increased affinity for ADP suggestive of 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).