Abstract
The tomato resistance gene Tm-22 encodes a coiled coil-nucleotide binding site-leucine rich repeat type resistance protein and confers effective immune response against tobamoviruses by detecting the presence of viral movement proteins (MPs). In this study, we show that the Nicotiana benthamiana Heat shock protein 90-kD (Hsp90) interacts with Tm-22. Silencing of Hsp90 reduced Tm-22-mediated resistance to Tobacco mosaic virus (TMV) and the steady-state levels of Tm-22 protein. Further, Hsp90 associates with SGT1 in yeast and in plant cells. These results suggest that Hsp90-SGT1 complex takes part in Tm-22-mediated TMV resistance by functioning as chaperone to regulate Tm-22 stability.
Highlights
In the natural environment, pathogen microbes, such as viruses, bacteria, fungi, oomycetes, and nematodes, can cause disease in host plants
Using high throughput viral-induced gene silencing (VIGS) assay, Heat shock protein 90-kD (Hsp90) was characterized to be a cofactor of Rx protein to stabilize its protein level (Lu et al, 2003)
We reported that Hsp90 directly interacts with Tm-22, a CC-nucleotide binding site (NBS)-leu-rich repeat (LRR) type of resistance protein, confers robust immune response against tobamoviruses
Summary
Pathogen microbes, such as viruses, bacteria, fungi, oomycetes, and nematodes, can cause disease in host plants. Some R genes can induce resistance response without visible HR (Heath, 2000; Jones and Dangl, 2006). A well-known example is the Rx gene from potato, which mediates extreme resistance against Potato virus X (PVX) without any visible cell death at the initial infection sites (Bendahmane et al, 1999). Tomato resistance gene Tm-22 can mediate extreme resistance against tobamoviruses (Zhang et al, 2013) They still have the potential to induce local cell death response in some conditions (Hall, 1980; Bendahmane et al, 1999; Du et al, 2013; Zhang et al, 2013)
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