Mediation of elicitin activity on tobacco is assumed by elicitin-sterol complexes.

Abstract:

:Elicitins secreted by phytopathogenic Phytophthora spp. are proteinaceous elicitors of plant defense mechanisms and were demonstrated to load, carry, and transfer sterols between membranes. The link between elicitor and sterol-loading properties was assessed with the use of site-directed mutagenesis of the 47 and 87 cryptogein tyrosine residues, postulated to be involved in sterol binding. Mutated cryptogeins were tested for their ability to load sterols, bind to plasma membrane putative receptors, and trigger biological responses. For each mutated elicitin, the chemical characterization of the corresponding complexes with stigmasterol (1:1 stoichiometry) demonstrated their full functionality. However, these proteins were strongly altered in their sterol-loading efficiency, specific binding to high-affinity sites, and activities on tobacco cells. Ligand replacement experiments strongly suggest that the formation of a sterol-elicitin complex is a requisite step before elicitins fasten to specific binding sites. This was confirmed with the use of two sterol-preloaded elicitins. Both more rapidly displaced labeled cryptogein from its specific binding sites than the unloaded proteins. Moreover, the binding kinetics of elicitins are related to their biological effects, which constitutes the first evidence that binding sites could be the biological receptors. The first event involved in elicitin-mediated cell responses is proposed to be the protein loading with a sterol molecule.

journal_name

Mol Biol Cell

authors

Osman H,Vauthrin S,Mikes V,Milat ML,Panabières F,Marais A,Brunie S,Maume B,Ponchet M,Blein JP

doi

10.1091/mbc.12.9.2825

keywords:

subject

Has Abstract

pub_date

2001-09-01 00:00:00

pages

2825-34

issue

9

eissn

1059-1524

issn

1939-4586

journal_volume

12

pub_type

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