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Titolo:
Mutational analysis of the Arabidopsis nucleotide binding site-leucine-rich repeat resistance gene RPS2
Autore:
Tao, Y; Yuan, FH; Leister, RT; Ausubel, FM; Katagiri, F;
Indirizzi:
Univ Maryland Baltimore Cty, Dept Sci Biol, Baltimore, MD 21250 USA Univ Maryland Baltimore Cty Baltimore MD USA 21250 altimore, MD 21250 USA Scripps Clin & Res Inst, Grad Program Macromol & Cellular Struct & Chem, La Jolla, CA 92037 USA Scripps Clin & Res Inst La Jolla CA USA 92037 hem, La Jolla, CA 92037 USA Novartis Agr Discovery Inst Inc, San Diego, CA 92121 USA Novartis Agr Discovery Inst Inc San Diego CA USA 92121 iego, CA 92121 USA Massachusetts Gen Hosp, Dept Mol Biol, Boston, MA 02114 USA Massachusetts Gen Hosp Boston MA USA 02114 Mol Biol, Boston, MA 02114 USA Harvard Univ, Sch Med, Dept Genet, Boston, MA 02114 USA Harvard Univ Boston MA USA 02114 ch Med, Dept Genet, Boston, MA 02114 USA
Titolo Testata:
PLANT CELL
fascicolo: 12, volume: 12, anno: 2000,
pagine: 2541 - 2554
SICI:
1040-4651(200012)12:12<2541:MAOTAN>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
PLANT-DISEASE RESISTANCE; ESCHERICHIA-COLI; AVIRULENCE GENE; CELL-DEATH; BACTERIAL; PROTEIN; TOMATO; THALIANA; SPECIFICITY; SECRETION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
43
Recensione:
Indirizzi per estratti:
Indirizzo: Katagiri, F Univ Maryland Baltimore Cty, Dept Sci Biol, Baltimore, MD 21250 USA Univ Maryland Baltimore Cty Baltimore MD USA 21250 21250 USA
Citazione:
Y. Tao et al., "Mutational analysis of the Arabidopsis nucleotide binding site-leucine-rich repeat resistance gene RPS2", PL CELL, 12(12), 2000, pp. 2541-2554

Abstract

Disease resistance proteins containing a nucleotide binding site (NBS) anda leucine-rich repeat (LRR) region compose the largest class of disease resistance proteins. These so-called NBS-LRR proteins confer resistance against a wide variety of phytopathogens. To help elucidate the mechanism by which NBS-LRR proteins recognize and transmit pathogen-derived signals, we analyzed mutant versions of the Arabidopsis NBS-LRR protein RPS2. The RPS2 gene confers resistance against Pseudomonas syringae strains carrying the avirulence gene avrRpt2. The activity of RPS2 derivatives in response to AvrRpt2 was measured by using a functional transient expression assay or by expressing the mutant proteins in transgenic plants. Directed mutagenesis revealed that the NBS and an N-terminal leucine zipper (LZ) motif were critical for RPS2 function. Mutations near the N terminus, including an LZ mutation, resulted in proteins that exhibited a dominant negative effect on wild-typeRPS2. Scanning the RPS2 molecule with a small in-frame internal deletion demonstrated that RPS2 does not have a large dispensable region. Overexpression of RPS2 in the transient assay in the absence of avrRpt2! also led to an apparent resistant response, presumably a consequence of a low basal activity of RPS2. The NBS and LZ were essential for this overdose effect, whereas the entire LRR was dispensable. RPSP interaction with a 75-kD protein (p75) required an N-terminal portion of RPSP that is smaller than the region required for the overdose effect. These findings illuminate the pathogen recognition mechanisms common among NBS-LRR proteins.

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Documento generato il 16/07/20 alle ore 16:45:31