2011
The role of sterol binding and surface charge in elicitin-induced resistance
LOCHMAN, Jan, Michal OBOŘIL, Veronika PLEŠKOVÁ, Kateřina DADÁKOVÁ, Nikola PTÁČKOVÁ et. al.Základní údaje
Originální název
The role of sterol binding and surface charge in elicitin-induced resistance
Název česky
Úloha vazby sterolu a povrchového náboje v biologické aktivitě elicitinů
Autoři
LOCHMAN, Jan, Michal OBOŘIL, Veronika PLEŠKOVÁ, Kateřina DADÁKOVÁ, Nikola PTÁČKOVÁ, Zbyněk ZDRÁHAL a Tomáš KAŠPAROVSKÝ
Vydání
10th conference of the EFPP “IPM 2.0" 2011
Další údaje
Jazyk
angličtina
Typ výsledku
Konferenční abstrakt
Obor
10600 1.6 Biological sciences
Stát vydavatele
Česká republika
Utajení
není předmětem státního či obchodního tajemství
Organizační jednotka
Přírodovědecká fakulta
Příznaky
Mezinárodní význam, Recenzováno
Změněno: 17. 1. 2013 16:44, doc. Mgr. Jan Lochman, Ph.D.
Anotace
V originále
Elicitins are family of small proteins secreted by species of the pathogenic fungus Phytophthora inducing a defence reaction in plants. On the basis of their pI they are classified as either alpha elicitins or more necrotizing beta elicitins. Cryptogein is beta elicitin secreted by Phytophthora cryptogea that can induce resistance to P. parasitica in tobacco plants. It contains a hydrophobic cavity capable of binding sterols and fatty acids and highly conserved omega-loop. On the basis of previous computer modelling experiments, by site-directed mutagenesis a series of cryptogein variants was prepared with altered abilities to bind lipids and with influenced surface charge. The sterol binding and phospholipids transfer activities corresponded well with the previously reported structural data. Induction of the synthesis of reactive oxygen species (ROS) in tobacco cells in suspension and proteomic analysis of intercellular fluid changes in tobacco leaves triggered by these mutant proteins were not proportional to their ability to bind or transfer sterols and phospholipids. However importance of omega-loop for interaction of the protein with the high affinity binding site on the plasma membrane was proved.
Návaznosti
CZ.1.07/2.4.00/31.0133, interní kód MU |
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GAP501/11/1003, projekt VaV |
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