Modulations of elicitins activity by changes in proteins
surface charge

p 2013

Modulations of elicitins activity by changes in proteins surface charge

LOCHMAN, Jan, Michal OBOŘIL, Jitka KLEMPOVÁ, Nikola PTÁČKOVÁ, Zbyněk ZDRÁHAL et. al.

Základní údaje

Originální název

Modulations of elicitins activity by changes in proteins surface charge

Název anglicky

Modulations of elicitins activity by changes in proteins surface charge

Autoři

LOCHMAN, Jan, Michal OBOŘIL, Jitka KLEMPOVÁ, Nikola PTÁČKOVÁ, Zbyněk ZDRÁHAL a Tomáš KAŠPAROVSKÝ

Vydání

World Biotechnology Congress - 2013, 2013

Další údaje

Typ výsledku

Vyžádané přednášky

Utajení

není předmětem státního či obchodního tajemství

Změněno: 1. 9. 2016 17:13, doc. Mgr. Jan Lochman, Ph.D.

Anotace

V originále

In plants, elicitins induce a hypersensitive response and non-specific systemic acquired resistance. They contain a hydrophobic cavity capable of binding sterols and fatty acids, and on the basis of their pI they are classified as either elicitins or more necrotizing elicitins. It has been assumed that conformational changes in the -loop evoke by sterol binding “activate” elicitins. However recent results suggest that the sterol-binding ability of elicitins associated with conformational changes in the -loop, might not be principal factors in elicitins biological activity and favour role of specific residues. The most probable candidates being lysine residues considering the previously observed correlation between necrotic index and pI together with a clear impact of the Lys13Val mutation in helix A on induction of a defence response in tobacco plants. In bioreactor a serious of cryptogein mutants with changed lysine residues was prepared. The significant impact of several mutations on cryptogein stability measured by differential scanning calorimetry was found. Moreover, some mutations alter the interaction of the protein with the binding site on the plasma membrane and the ability to induce a hypersensitive response and resistance. Determined results provide possibility to specifically modulate elicitins biological activity though the mutation of specific residues.

Návaznosti

GAP501/11/1003, projekt VaV

Název: Interakce mutantních forem cryptogeinu s membránovým vazebným místem: charakterizace pomocí biosensorů

Investor: Grantová agentura ČR, Interactions of mutant forms of cryptogein with a membrane binding site: biosensors-based characterisation

Citovat

LOCHMAN, Jan, Michal OBOŘIL, Jitka KLEMPOVÁ, Nikola PTÁČKOVÁ, Zbyněk ZDRÁHAL a Tomáš KAŠPAROVSKÝ. Modulations of elicitins activity by changes in proteins surface charge. In World Biotechnology Congress - 2013. 2013.

@misc{1352858,
   author = {Lochman, Jan and Obořil, Michal and Klempová, Jitka and Ptáčková, Nikola and Zdráhal, Zbyněk and Kašparovský, Tomáš},
   booktitle = {World Biotechnology Congress - 2013},
   title = {Modulations of elicitins activity by changes in proteins surface charge},
   year = {2013}
}

TY  - SLIDE
ID  - 1352858
AU  - Lochman, Jan - Obořil, Michal - Klempová, Jitka - Ptáčková, Nikola - Zdráhal, Zbyněk - Kašparovský, Tomáš
PY  - 2013
TI  - Modulations of elicitins activity by changes in proteins surface charge
N2  - In plants, elicitins induce a hypersensitive response and non-specific systemic acquired resistance. They contain a hydrophobic cavity capable of binding sterols and fatty acids, and on the basis of their pI they are classified as either elicitins or more necrotizing elicitins. It has been assumed that conformational changes in the -loop evoke by sterol binding “activate” elicitins. However recent results suggest that the sterol-binding ability of elicitins associated with conformational changes in the -loop, might not be principal factors in elicitins biological activity and favour role of specific residues. The most probable candidates being lysine residues considering the previously observed correlation between necrotic index and pI together with a clear impact of the Lys13Val mutation in helix A on induction of a defence response in tobacco plants. In bioreactor a serious of cryptogein mutants with changed lysine residues was prepared. The significant impact of several mutations on cryptogein stability measured by differential scanning calorimetry was found. Moreover, some mutations alter the interaction of the protein with the binding site on the plasma membrane and the ability to induce a hypersensitive response and resistance. Determined results provide possibility to specifically modulate elicitins biological activity though the mutation of specific residues.
ER  -

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