Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Six amino acid changes confined to the leucine-rich repeat beta-strand/beta-turn motif determine the difference between the P and P2 rust resistance specificities in flax
Autore:
Dodds, PN; Lawrence, GJ; Ellis, JG;
Indirizzi:
CSIRO, Canberra, ACT 2601, Australia CSIRO Canberra ACT Australia 2601CSIRO, Canberra, ACT 2601, Australia
Titolo Testata:
PLANT CELL
fascicolo: 1, volume: 13, anno: 2001,
pagine: 163 - 178
SICI:
1040-4651(200101)13:1<163:SAACCT>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
DOWNY MILDEW RESISTANCE; FOR-GENE CONCEPT; AVIRULENCE DETERMINANTS; PERONOSPORA-PARASITICA; DIVERGENT SELECTION; OXALATE OXIDASE; ARABIDOPSIS; LOCUS; TOMATO; PROTEINS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
44
Recensione:
Indirizzi per estratti:
Indirizzo: Ellis, JG CSIRO, GPO Box 1500, Canberra, ACT 2601, Australia CSIRO GPO Box1500 Canberra ACT Australia 2601 T 2601, Australia
Citazione:
P.N. Dodds et al., "Six amino acid changes confined to the leucine-rich repeat beta-strand/beta-turn motif determine the difference between the P and P2 rust resistance specificities in flax", PL CELL, 13(1), 2001, pp. 163-178

Abstract

At least six rust resistance specificities (P and P1 to P5) map to the complex P locus in flax. The P2 resistance gene was identified by transposon tagging and transgenic expression. P2 is a member of a small multigene family and encodes a protein with,nucleotide binding site (NBS) and leucine-richrepeat (LRR) domains and an N-terminal Toll/interleukin-1 receptor (TIR) homology domain, as well as a C-terminal non-LRR (CNL) domain of similar to 150 amino acids. A related CNL domain was detected in almost half of the predicted Arabidopsis TIR-NBS-LRR sequences, including the RPS4 and RPP1 resistance proteins, and in the tobacco N protein, but not in the flax L and M proteins, Presence or absence of this domain defines two subclasses of TIR-NBS-LRR resistance genes, Truncations of the P2 CNL domain cause loss of function, and evidence for diversifying selection was detected in this domain, suggesting a possible role in specificity determination. A spontaneous rust-susceptible mutant of P2 contained a G-->E amino acid substitution in the GLPL motif, which is conserved in the NBS domains of plant resistance proteins and the animal cell death control proteins APAF-1 and CED4, providingdirect evidence for the importance of this motif in resistance gene function. A P2 homologous gene isolated from a flax line expressing the P resistance specificity encodes a protein with only 10 amino acid differences from the P2 protein. Chimeric gene constructs indicate that just six of these amino acid changes, all located within the predicted beta -strand/beta -turn motif of four LRR units, are sufficient to alter P2 to the P specificity.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/07/20 alle ore 08:37:19