Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 399621
Title Nucleocytoplasmic distribution is required for activation of resistance by the potato NB-LRR receptor Rx1 and is balanced by its functional domains
Author(s) Slootweg, E.J.; Roosien, J.; Spiridon, L.N.; Petrescu, A.J.; Tameling, W.I.L.; Joosten, M.H.A.J.; Pomp, H.; Schaik, C.C. van; Dees, R.H.L.; Borst, J.W.; Smant, G.; Schots, A.; Bakker, J.; Goverse, A.
Source The Plant Cell 22 (2010)12. - ISSN 1040-4651 - p. 4195 - 4215.
DOI http://dx.doi.org/10.1105/tpc.110.077537
Department(s) Laboratory of Nematology
Laboratory of Phytopathology
Flower Bulbs
Biochemistry
EPS-2
Publication type Refereed Article in a scientific journal
Publication year 2010
Keyword(s) secondary structure prediction - plant-disease resistance - nuclear-localization signals - green fluorescent protein - innate immune-response - leucine-rich repeat - to-cell movement - virus-x - arabidopsis-thaliana - coat protein
Abstract The Rx1 protein, as many resistance proteins of the nucleotide binding–leucine-rich repeat (NB-LRR) class, is predicted to be cytoplasmic because it lacks discernable nuclear targeting signals. Here, we demonstrate that Rx1, which confers extreme resistance to Potato virus X, is located both in the nucleus and cytoplasm. Manipulating the nucleocytoplasmic distribution of Rx1 or its elicitor revealed that Rx1 is activated in the cytoplasm and cannot be activated in the nucleus. The coiled coil (CC) domain was found to be required for accumulation of Rx1 in the nucleus, whereas the LRR domain promoted the localization in the cytoplasm. Analyses of structural subdomains of the CC domain revealed no autonomous signals responsible for active nuclear import. Fluorescence recovery after photobleaching and nuclear fractionation indicated that the CC domain binds transiently to large complexes in the nucleus. Disruption of the Rx1 resistance function and protein conformation by mutating the ATP binding phosphate binding loop in the NB domain, or by silencing the cochaperone SGT1, impaired the accumulation of Rx1 protein in the nucleus, while Rx1 versions lacking the LRR domain were not affected in this respect. Our results support a model in which interdomain interactions and folding states determine the nucleocytoplasmic distribution of Rx1
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