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Author
S. Fenyk
P.D. Townsend
C.H. Dixon
G.B. Spies
A. de San Eustaquio Campillo
E.J. Slootweg
L.B. Westerhof
F.K.K. Gawehns
M.R. Knight
G.J. Sharples
A. Goverse
L.O. Pålsson
F.L.W. Takken
M.J. Cann
Year
2015
Title
The Potato Nucleotide-binding Leucine-rich Repeat (NLR) Immune Receptor Rx1 Is a Pathogen-dependent DNA-deforming Protein
Journal
The Journal of Biological Chemistry
Volume | Issue number
290 | 41
Pages (from-to)
24945-24960
Number of pages
16
Document type
Article
Faculty
Faculty of Science (FNWI)
Institute
Swammerdam Institute for Life Sciences (SILS)
Abstract
Plant nucleotide-binding leucine-rich repeat (NLR) proteins enable cells to respond to pathogen attack. Several NLRs act in the nucleus; however, conserved nuclear targets that support their role in immunity are unknown. Previously, we noted a structural homology between the nucleotide-binding domain of NLRs and DNA replication origin-binding Cdc6/Orc1 proteins. Here we show that the NB-ARC (nucleotide-binding, Apaf-1, R-proteins, and CED-4) domain of the Rx1 NLR of potato binds nucleic acids. Rx1 induces ATP-dependent bending and melting of DNA in vitro, dependent upon a functional P-loop. In situ full-length Rx1 binds nuclear DNA following activation by its cognate pathogen-derived effector protein, the coat protein of potato virus X. In line with its obligatory nucleocytoplasmic distribution, DNA binding was only observed when Rx1 was allowed to freely translocate between both compartments and was activated in the cytoplasm. Immune activation induced by an unrelated NLR-effector pair did not trigger an Rx1-DNA interaction. DNA binding is therefore not merely a consequence of immune activation. These data establish a role for DNA distortion in Rx1 immune signaling and define DNA as a molecular target of an activated NLR.
URL
go to publisher's site
Language
English
Permalink
http://hdl.handle.net/11245/1.492735
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  • The Potato Nucleotide-binding Leucine-rich Repeat

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