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

J 2011

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

PLEŠKOVÁ, Veronika, Tomáš KAŠPAROVSKÝ, Michal OBOŘIL, Nikola PTÁČKOVÁ, Radka CHALOUPKOVÁ et. al.

Základní údaje

Originální název

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

Autoři

PLEŠKOVÁ, Veronika (203 Česká republika, domácí), Tomáš KAŠPAROVSKÝ (203 Česká republika, domácí), Michal OBOŘIL (203 Česká republika, domácí), Nikola PTÁČKOVÁ (203 Česká republika, domácí), Radka CHALOUPKOVÁ (203 Česká republika, domácí), Ladislav DOKLÁDAL (203 Česká republika, domácí), Jiří DAMBORSKÝ (203 Česká republika, domácí) a Jan LOCHMAN (203 Česká republika, garant, domácí)

Vydání

Plant Physiology and Biochemistry, Elsevier, 2011, 0981-9428

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Nizozemské království

Utajení

není předmětem státního či obchodního tajemství

Impakt faktor

Impact factor: 2.838

Kód RIV

RIV/00216224:14310/11:00052011

Organizační jednotka

Přírodovědecká fakulta

DOI

http://dx.doi.org/10.1016/j.plaphy.2011.01.008

UT WoS

000288777300012

Klíčová slova anglicky

Elicitins; Surface charge; Membrane interaction; Lipid binding; Resistance induction

Štítky

AKR, rivok

Změněno: 20. 4. 2012 10:11, Ing. Andrea Mikešková

Anotace

V originále

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. Compared to wild type cryptogein, mutation Lys13Val resulted in lowered expression of defence related genes and compromised resistance to P. parasitica. Furthermore, resistance induced by Lys13Val mutant was similar to that induced by acidic elicitin capsicein containing at amino position 13. valine. Determined results sustained a crucial role of positive lysine residues on the surface of basic elicitins and suggested their significant role in correct protein-membrane interaction and thus on their biological activity.

Návaznosti

ED0001/01/01, projekt VaV

Název: CETOCOEN

MSM0021622412, záměr

Název: Interakce mezi chemickými látkami, prostředím a biologickými systémy a jejich důsledky na globální, regionální a lokální úrovni (INCHEMBIOL) (Akronym: INCHEMBIOL)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Interakce mezi chemickými látkami, prostředím a biologickými systémy a jejich důsledky na globální , regionální a lokální úrovni

MSM0021622413, záměr

Název: Proteiny v metabolismu a při interakci organismů s prostředím

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Proteiny v metabolismu a při interakci organismů s prostředím

Citovat

PLEŠKOVÁ, Veronika, Tomáš KAŠPAROVSKÝ, Michal OBOŘIL, Nikola PTÁČKOVÁ, Radka CHALOUPKOVÁ, Ladislav DOKLÁDAL, Jiří DAMBORSKÝ a Jan LOCHMAN. Elicitine-membrane interaction is driven by a positive charge on the protein surface: Role of Lys13 residue in lipids loading and resistance induction. Plant Physiology and Biochemistry. Elsevier, 2011, roč. 49, č. 3, s. 321-328. ISSN 0981-9428. Dostupné z: https://dx.doi.org/10.1016/j.plaphy.2011.01.008.

@article{931239,
   author = {Plešková, Veronika and Kašparovský, Tomáš and Obořil, Michal and Ptáčková, Nikola and Chaloupková, Radka and Dokládal, Ladislav and Damborský, Jiří and Lochman, Jan},
   article_number = {3},
   doi = {http://dx.doi.org/10.1016/j.plaphy.2011.01.008},
   keywords = {Elicitins; Surface charge; Membrane interaction; Lipid binding; Resistance induction},
   language = {eng},
   issn = {0981-9428},
   journal = {Plant Physiology and Biochemistry},
   title = {Elicitine-membrane interaction is driven by a positive charge on the protein surface: Role of Lys13 residue in lipids loading and resistance induction},
   volume = {49},
   year = {2011}
}

TY  - JOUR
ID  - 931239
AU  - Plešková, Veronika - Kašparovský, Tomáš - Obořil, Michal - Ptáčková, Nikola - Chaloupková, Radka - Dokládal, Ladislav - Damborský, Jiří - Lochman, Jan
PY  - 2011
TI  - Elicitine-membrane interaction is driven by a positive charge on the protein surface: Role of Lys13 residue in lipids loading and resistance induction
JF  - Plant Physiology and Biochemistry
VL  - 49
IS  - 3
SP  - 321-328
EP  - 321-328
PB  - Elsevier
SN  - 09819428
KW  - Elicitins
KW  - Surface charge
KW  - Membrane interaction
KW  - Lipid binding
KW  - Resistance induction
N2  - 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. Compared to wild type cryptogein, mutation Lys13Val resulted in lowered expression of defence related genes and compromised resistance to P. parasitica. Furthermore, resistance induced by Lys13Val mutant was similar to that induced by acidic elicitin capsicein containing at amino position 13. valine. Determined results sustained a crucial role of positive lysine residues on the surface of basic elicitins and suggested their significant role in correct protein-membrane interaction and thus on their biological activity.
ER  -

PLEŠKOVÁ, Veronika, Tomáš KAŠPAROVSKÝ, Michal OBOŘIL, Nikola PTÁČKOVÁ, Radka CHALOUPKOVÁ, Ladislav DOKLÁDAL, Jiří DAMBORSKÝ a Jan LOCHMAN. Elicitine-membrane interaction is driven by a positive charge on the protein surface: Role of Lys13 residue in lipids loading and resistance induction. \textit{Plant Physiology and Biochemistry}. Elsevier, 2011, roč.~49, č.~3, s.~321-328. ISSN~0981-9428. Dostupné z: https://dx.doi.org/10.1016/j.plaphy.2011.01.008.

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