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 424955
Title Dual regulatory roles of the extended N-terminus for activation of the tomato Mi-1.2 resistance protein
Author(s) Lukasik-Shreepaathy, E.; Slootweg, E.J.; Richter, H.; Cornelissen, B.J.C.; Goverse, A.; Takken, F.L.W.
Source Molecular Plant-Microbe Interactions 25 (2012)8. - ISSN 0894-0282 - p. 1045 - 1057.
DOI https://doi.org/10.1094/MPMI-11-11-0302
Department(s) Laboratory of Nematology
EPS-2
Publication type Refereed Article in a scientific journal
Publication year 2012
Keyword(s) secondary structure prediction - rich repeat domain - cell-death - nucleotide-binding - disease resistance - confers resistance - immune-system - coiled coils - lrr protein - arc domain
Abstract Plant resistance (R) proteins mediate race-specific immunity and initiate host defenses that are often accompanied by a localized cell-death response. Most R proteins belong to the NB-LRR protein family as they carry a central NB-ARC domain fused to an LRR domain. The CC domain at the N-terminus of some Solanaceous NB-LRR proteins is extended with a solanaceae domain (SD). Tomato Mi-1.2, which confers resistance against nematodes, white flies, psyllids and aphids, encodes a typical SD-CNL protein. Here, we analyzed the role of the extended N-terminus for Mi-1.2 activation. Removal of the first part of the N-terminus (Nt1) induced Mi-1.2-mediated cell death that could be suppressed by over-expression of the second half of the N-terminal region (Nt2). Yet, autoactivating NB-ARC-LRR mutants require in trans co-expression of the N-terminal region to induce cell death, indicating that the N-terminus functions both as a negative and a positive regulator. Based on secondary structure predictions we could link both functions to three distinct subdomains; a typical CC domain and two novel, structurally-conserved helical subdomains called SD1 and SD2. A negative regulatory function could be assigned to the SD1 whereas SD2 and the CC together function as positive regulators of Mi-1.2 mediated cell death
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