Elicitine-membrane interaction is driven by a positive charge on the protein surface: Role of Lys13 residue in lipids loading and resistance induction

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F11%3A00052011" target="_blank" >RIV/00216224:14310/11:00052011 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.plaphy.2011.01.008" target="_blank" >http://dx.doi.org/10.1016/j.plaphy.2011.01.008</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.plaphy.2011.01.008" target="_blank" >10.1016/j.plaphy.2011.01.008</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Elicitine-membrane interaction is driven by a positive charge on the protein surface: Role of Lys13 residue in lipids loading and resistance induction

Popis výsledku v původním jazyce

Elicitins are family of small proteins secreted by species of the pathogenic fungus Phytophthora inducing a defence reaction in plants. They contain a hydrophobic cavity capable of binding sterols and fatty acids, and on the basis of their pI they are classified as either alfa elicitins or more necrotizing beta elicitins. The residue Lys13 was previously identified as a key determinant of the necrotising activity of basic elicitins. In the present study we describe changes in the ability of cryptogein,a beta elicitin inducing a hypersensitive response in tobacco, to transfer sterols and fatty acids between micelles and liposomes upon Lys13Val mutation. We propose that the change in activity is influenced by the elimination of positive charge on the surface of cryptogein, which is significant for correct positioning of the protein during lipid loading, without adversely affecting the binding of sterol to the cavity of the protein.

Název v anglickém jazyce

Elicitine-membrane interaction is driven by a positive charge on the protein surface: Role of Lys13 residue in lipids loading and resistance induction

Popis výsledku anglicky

Elicitins are family of small proteins secreted by species of the pathogenic fungus Phytophthora inducing a defence reaction in plants. They contain a hydrophobic cavity capable of binding sterols and fatty acids, and on the basis of their pI they are classified as either alfa elicitins or more necrotizing beta elicitins. The residue Lys13 was previously identified as a key determinant of the necrotising activity of basic elicitins. In the present study we describe changes in the ability of cryptogein,a beta elicitin inducing a hypersensitive response in tobacco, to transfer sterols and fatty acids between micelles and liposomes upon Lys13Val mutation. We propose that the change in activity is influenced by the elimination of positive charge on the surface of cryptogein, which is significant for correct positioning of the protein during lipid loading, without adversely affecting the binding of sterol to the cavity of the protein.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/ED0001%2F01%2F01" target="_blank" >ED0001/01/01: CETOCOEN</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)<br>S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2011

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Plant Physiology and Biochemistry

ISSN

0981-9428

e-ISSN

—

Svazek periodika

49

Číslo periodika v rámci svazku

3

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

8

Strana od-do

321-328

Kód UT WoS článku

000288777300012

EID výsledku v databázi Scopus

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