Malondialdehyde enhances PsbP protein release during heat stress in Arabidopsis

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F23%3A73620680" target="_blank" >RIV/61989592:15310/23:73620680 - isvavai.cz</a>

Výsledek na webu

<a href="https://www.sciencedirect.com/science/article/pii/S0981942823004953" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0981942823004953</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.plaphy.2023.107984" target="_blank" >10.1016/j.plaphy.2023.107984</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Malondialdehyde enhances PsbP protein release during heat stress in Arabidopsis

Popis výsledku v původním jazyce

Under environmental conditions, plants are exposed to various abiotic and biotic stress factors, which commonly cause the oxidation of lipids and proteins. Lipid peroxidation constantly produces malondialdehyde (MDA), a secondary product of lipid peroxidation, which is covalently bound to proteins forming MDA-protein adducts. The spatial distribution of MDA-protein adducts in Arabidopsis leaves shows that MDA-protein adducts are located in the chloroplasts, uniformly spread out over the thylakoid membrane. At the lumenal side of thylakoid membrane, MDA interacts with PsbP, an extrinsic subunit of the photosystem II (PSII), which is in electrostatic interaction with the PSII core proteins. Under heat stress, when MDA is moderately enhanced, the electrostatic interaction between PsbP and PSII core proteins is weakened, and PsbP with bound MDA is released in the lumen. It is proposed here that the electrophilic MDA is bound to the nucleophilic lysine residues of PsbP, which are involved in electrostatic interactions with the negatively charged glutamate of the PSII core protein. Our data provide crucial information about the MDA binding topology in the higher plant PSII complex, which is necessary to understand better the physiological functions of MDA for plant survival under stress.

Název v anglickém jazyce

Malondialdehyde enhances PsbP protein release during heat stress in Arabidopsis

Popis výsledku anglicky

Under environmental conditions, plants are exposed to various abiotic and biotic stress factors, which commonly cause the oxidation of lipids and proteins. Lipid peroxidation constantly produces malondialdehyde (MDA), a secondary product of lipid peroxidation, which is covalently bound to proteins forming MDA-protein adducts. The spatial distribution of MDA-protein adducts in Arabidopsis leaves shows that MDA-protein adducts are located in the chloroplasts, uniformly spread out over the thylakoid membrane. At the lumenal side of thylakoid membrane, MDA interacts with PsbP, an extrinsic subunit of the photosystem II (PSII), which is in electrostatic interaction with the PSII core proteins. Under heat stress, when MDA is moderately enhanced, the electrostatic interaction between PsbP and PSII core proteins is weakened, and PsbP with bound MDA is released in the lumen. It is proposed here that the electrophilic MDA is bound to the nucleophilic lysine residues of PsbP, which are involved in electrostatic interactions with the negatively charged glutamate of the PSII core protein. Our data provide crucial information about the MDA binding topology in the higher plant PSII complex, which is necessary to understand better the physiological functions of MDA for plant survival under stress.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10610 - Biophysics

Projekt

<a href="/cs/project/EF16_019%2F0000827" target="_blank" >EF16_019/0000827: Rostliny jako prostředek udržitelného globálního rozvoje</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2023

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

1873-2690

Svazek periodika

202

Číslo periodika v rámci svazku

SEP

Stát vydavatele periodika

FR - Francouzská republika

Počet stran výsledku

9

Strana od-do

"107984-1"-"107984-9"

Kód UT WoS článku

001072491700001

EID výsledku v databázi Scopus

2-s2.0-85169556028