High affinity binding of a fungal oligopeptide elicitor to parsley plasma membranes triggers multiple defense responses.
Cell
; 78(3): 449-60, 1994 Aug 12.
Article
en En
| MEDLINE
| ID: mdl-8062387
ABSTRACT
An oligopeptide of 13 amino acids (Pep-13) identified within a 42 kDa glycoprotein elicitor from P. mega-sperma was shown to be necessary and sufficient to stimulate a complex defense response in parsley cells comprising H+/Ca2+ influxes, K+/Cl- effluxes, an oxidative burst, defense-related gene activation, and phytoalexin formation. Binding of radiolabeled Pep-13 to parsley microsomes and protoplasts was specific, reversible, and saturable. Identical structural features of Pep-13 were found to be responsible for specific binding and initiation of all plant responses analyzed. The high affinity binding site recognizing the peptide ligand (KD = 2.4 nM) may therefore represent a novel class of receptors in plants, and the rapidly induced ion fluxes may constitute elements of the signal transduction cascade triggering pathogen defense in plants.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Oligopéptidos
/
Phytophthora
/
Verduras
/
Glicoproteínas
/
Transducción de Señal
/
Membrana Celular
Idioma:
En
Revista:
Cell
Año:
1994
Tipo del documento:
Article