|
|
|
RESEARCH PAPER
1 Departamento de Bioquímica e Biologia Molecular/BIOGRO/UFV, 36571.000, Viçosa, MG, Brazil; 2 Howard Hughes Medical Institute and Plant Biology Laboratory, The Salk Institute for Biological Studies, La Jolla, California 92037, USA
Despite the large number of leucine-rich-repeat (LRR) receptor-like-kinases (RLKs) in plants and their conceptual relevance in signaling events, functional information is restricted to a few family members. Here we describe the characterization of new LRR-RLK family members as virulence targets of the geminivirus nuclear shuttle protein (NSP). NSP interacts specifically with three LRR-RLKs, NIK1, NIK2, and NIK3, through an 80-amino acid region that encompasses the kinase active site and A-loop. We demonstrate that these NSP-interacting kinases (NIKs) are membrane-localized proteins with biochemical properties of signaling receptors. They behave as authentic kinase proteins that undergo autophosphorylation and can also phosphorylate exogenous substrates. Autophosphorylation occurs via an intermolecular event and oligomerization precedes the activation of the kinase. Binding of NSP to NIK inhibits its kinase activity in vitro, suggesting that NIK is involved in antiviral defense response. In support of this, infectivity assays showed a positive correlation between infection rate and loss of NIK1 and NIK3 function. Our data are consistent with a model in which NSP acts as a virulence factor to suppress NIK-mediated antiviral responses.
[Keywords: Receptor-like kinases; nuclear shuttle protein; geminivirus; defense signaling]
Received August 3, 2004; revised version accepted August 23, 2004.
3 Corresponding author. E-MAIL bbfontes{at}ufv.br; FAX 55-31-3899-2864.
![]()
CiteULike
Connotea
Del.icio.us
Digg
Reddit
Technorati What's this?
This article has been cited by other articles:
![]() |
H. Gherbi, K. Markmann, S. Svistoonoff, J. Estevan, D. Autran, G. Giczey, F. Auguy, B. Peret, L. Laplaze, C. Franche, et al. From the Cover: SymRK defines a common genetic basis for plant root endosymbioses with arbuscular mycorrhiza fungi, rhizobia, and Frankiabacteria PNAS, March 25, 2008; 105(12): 4928 - 4932. [Abstract] [Full Text] [PDF] |
||||
![]() |
A. Marmagne, M. Ferro, T. Meinnel, C. Bruley, L. Kuhn, J. Garin, H. Barbier-Brygoo, and G. Ephritikhine A High Content in Lipid-modified Peripheral Proteins and Integral Receptor Kinases Features in the Arabidopsis Plasma Membrane Proteome Mol. Cell. Proteomics, November 1, 2007; 6(11): 1980 - 1996. [Abstract] [Full Text] [PDF] |
||||
![]() |
W. Shen and L. Hanley-Bowdoin Geminivirus Infection Up-Regulates the Expression of Two Arabidopsis Protein Kinases Related to Yeast SNF1- and Mammalian AMPK-Activating Kinases Plant Physiology, December 1, 2006; 142(4): 1642 - 1655. [Abstract] [Full Text] [PDF] |
||||
![]() |
L. H. Florentino, A. A. Santos, M. R. Fontenelle, G. L. Pinheiro, F. M. Zerbini, M. C. Baracat-Pereira, and E. P. B. Fontes A PERK-Like Receptor Kinase Interacts with the Geminivirus Nuclear Shuttle Protein and Potentiates Viral Infection. J. Virol., July 1, 2006; 80(13): 6648 - 6656. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. F. Carvalho, R. Turgeon, and S. G. Lazarowitz The Geminivirus Nuclear Shuttle Protein NSP Inhibits the Activity of AtNSI, a Vascular-Expressed Arabidopsis Acetyltransferase Regulated with the Sink-to-Source Transition Plant Physiology, April 1, 2006; 140(4): 1317 - 1330. [Abstract] [Full Text] [PDF] |
||||