Query:
faculty: "FNWI" and publication year: "2002"
| Authors | W.I.L. Tameling, S.D.J. Elzinga, P.S. Darmin, J.H. Vossen, F.L.W. Takken, M.A. Haring, B.J.C. Cornelissen | | Title | The tomato R gene products I-2 and Mi-1 are functional ATP binding proteins with ATPase activity |
| Journal | The Plant Cell |
| Volume | 14 |
| Year | 2002 |
| Pages | 2929-2939 |
| ISSN | 10404651 |
| Faculty | Faculty of Science |
| Institute/dept. | FNWI: Swammerdam Institute for Life Sciences (SILS) |
| Keywords | ATP binding proteins; Tomato R proteins |
| 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 NBSLRR class, we propose that they all are capable of binding and hydrolyzing ATP. |
| Document type | Article |
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