An autoactive mutant of the M flax rust resistance protein has a preference for binding ATP, whereas wild-type M protein binds ADP

Williams, Simon J., Sornaraj, Pradeep, deCourcy-Ireland, Emma, Menz, R. Ian, Kobe, Bostjan, Ellis, Jeffrey G., Dodds, Peter N. and Anderson, Peter A. (2011) An autoactive mutant of the M flax rust resistance protein has a preference for binding ATP, whereas wild-type M protein binds ADP. Molecular Plant-Microbe Interactions, 24 8: 897-906. doi:10.1094/MPMI-03-11-0052


Author Williams, Simon J.
Sornaraj, Pradeep
deCourcy-Ireland, Emma
Menz, R. Ian
Kobe, Bostjan
Ellis, Jeffrey G.
Dodds, Peter N.
Anderson, Peter A.
Title An autoactive mutant of the M flax rust resistance protein has a preference for binding ATP, whereas wild-type M protein binds ADP
Journal name Molecular Plant-Microbe Interactions   Check publisher's open access policy
ISSN 0894-0282
1943-7706
Publication date 2011-08
Sub-type Article (original research)
DOI 10.1094/MPMI-03-11-0052
Volume 24
Issue 8
Start page 897
End page 906
Total pages 10
Place of publication St. Paul, MN, U.S.A.
Publisher American Phytopathological Society
Collection year 2012
Language eng
Formatted abstract Resistance (R) proteins are key regulators of the plant innate immune system and are capable of pathogen detection and activation of the hypersensitive cell death immune response. To understand the molecular mechanism of R protein activation, we undertook a phenotypic and biochemical study of the flax nucleotide binding (NB)-ARC leucine-rich repeat protein, M. Using Agrobacterium-mediated transient expression in flax cotyledons, site-directed mutations of key residues within the P-loop, kinase 2, and MHD motifs within the NB-ARC domain of M were shown to affect R protein function. When purified using a yeast expression system and assayed for ATP and ADP, these mutated proteins exhibited marked differences in the quantity and identity of the bound nucleotide. ADP was bound to recombinant wild-type M protein, while the nonfunctional P-loop mutant did not have any nucleotides bound. In contrast, ATP was bound to an autoactive M protein mutated in the highly conserved MHD motif. These data provide direct evidence supporting a model of R protein function in which the “off” R protein binds ADP and activation of R protein defense signaling involves the exchange of ADP for ATP.
Keyword NB-ARC domain
Plant-pathogen interactions
Programmed cell-death
Rich repeat protein
Hypersensitive response
Nucleotide exchange
Gene-products
Activation
Hydrolysis
Apaf-1
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2012 Collection
School of Chemistry and Molecular Biosciences
Institute for Molecular Bioscience - Publications
 
Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 21 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 22 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Access Statistics: 95 Abstract Views  -  Detailed Statistics
Created: Sun, 21 Aug 2011, 02:14:10 EST by System User on behalf of School of Chemistry & Molecular Biosciences