The tomato R gene products I-2 and MI-1 are functional ATP binding proteins with ATPase activity.
| Publication details |
| Title | The tomato R gene products I-2 and MI-1 are functional ATP binding proteins with ATPase activity. |
| Series name | The Plant cell |
| Volume | 14 |
| Issue | 11 |
| Year | 2002 |
| Pages | 2929-39 |
| Authors | Tameling, WI. Elzinga, SD. Darmin, PS. Vossen, JH. Takken, FL. Haring, MA. Cornelissen, BJ |
| Abstract | Most plant disease resistance (R) genes known today encode proteins with a central nucleotide binding site (NBS) and a C-terminal Leu-rich repeat (LRR) domain. The NBS contains three ATP/GTP binding motifs known as the kinase-1a or P-loop, kinase-2, and kinase-3a motifs. In this article, we show that the NBS of R proteins forms a functional nucleotide binding pocket. The N-terminal halves of two tomato R proteins, I-2 conferring resistance to Fusarium oxysporum and Mi-1 conferring resistance to root-knot nematodes and potato aphids, were produced as glutathione S-transferase fusions in Escherichia coli. In a filter binding assay, purified I-2 was found to bind ATP rather than other nucleoside triphosphates. ATP binding appeared to be fully dependent on the presence of a divalent cation. A mutant I-2 protein containing a mutation in the P-loop showed a strongly reduced ATP binding capacity. Thin layer chromatography revealed that both I-2 and Mi-1 exerted ATPase activity. Based on the strong conservation of NBS domains in R proteins of the NBS-LRR class, we propose that they all are capable of binding and hydrolyzing ATP. |
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