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.

Basic information

Original name

Modulations of elicitins activity by changes in proteins surface charge

Name (in English)

Modulations of elicitins activity by changes in proteins surface charge

Authors

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

Edition

World Biotechnology Congress - 2013, 2013

Other information

Type of outcome

Vyžádané přednášky

Confidentiality degree

není předmětem státního či obchodního tajemství

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

Abstract

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.

Links

GAP501/11/1003, research and development project

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

Investor: Czech Science Foundation

Citovat

LOCHMAN, Jan, Michal OBOŘIL, Jitka KLEMPOVÁ, Nikola PTÁČKOVÁ, Zbyněk ZDRÁHAL and 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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